Publications - Tsutomu Arakawa

Arakawa, T., Tokunaga, H., Tokunaga, M., and Yamaguchi, R. (2016). Unique features of halophilic proteins. Curr. Protein Pept. Sci., epub ahead of print

Yoshizawa, S., Arakawa, T., and Shiraki, K. (2016). Effect of counter ions of arginine as an additive for the solubilization of protein and aromatic compounds. Int. J. Biol. Macromol. 91, 471-476.

Miyatake, T., Yoshizawa, S., Arakawa, T., and Shiraki, K. (2016). Charge state of arginine as an additive on heat-induced protein aggregation. Int. J. Biol. Macromol. 87, 563-569.

Arakawa, T., Ponce, S., and Young, G. (2015). Isoform separation of proteins by mixed-mode chromatography. Protein Expr. Purif. 116, 144-151.

Hirano, A., Arakawa, T., and Kameda, T. (2015). Effects of arginine on multimodal anion exchange chromatography. Protein Expr. Purif. 116, 105-112.

Shimada, M., Takai, E., Ejima, D., Arakawa, T., and Shiraki, K. (2015). Heat-induced formation of myosin oligomer-soluble filament complex in high-salt solution. Int. J. Biol. Macromol. 73, 17-22.

Arakawa, T. and Kita, Y. (2014). Multi-Faceted Arginine: Mechanism of the Effects of Arginine on Protein. Curr. Protein Pept. Sci. 15, 608-620.

Arakawa, T., Tsumoto, K., and Ejima, D. (2014). Alternative downstream processes for production of antibodies and antibody fragments. Biochim. Biophys. Acta 18, 2032-2040.

Hirano, A., Maruyama, T., Shiraki, K., Arakawa, T., and Kameda, T. (2014). Mechanism of protein desorption from 4-mercaptoethylpyridine resins by arginine solutions. J. Chromatogr. A 1373, 141-148.

Mizukami, M., Tokunaga, H., Onishi, H., Ueno, Y., Hanagata, H., Miyazaki, N., Kiyose, N., Ito, Y., Ishibashi, M., Hagihara, Y., Arakawa, T., Miyauchi, A., and Tokunaga, M. (2014). Highly efficient production of VHH antibody fragments in Brevibacillus choshinensis expression system. Protein Expr. Purif. 105C, 23-32.

Yoshizawa, S., Arakawa, T., and Shiraki, K. (2014). Dependence of ethanol effects on protein charges. Int. J. Biol Macromol. 68, 169-172.

Arakawa, T., Niikura, T., and Kita, Y. (2014). Inactive C8Ahumanin analog is as stable as a potent S14Ghumanin analog. Mol. Med. Rep. 9, 375-379.

Hirano, A., Arakawa, T., and Kameda, T. (2014). Interaction of arginine with Capto MMC in multimodal chromatography. J. Chromatogr. A 1338, 58-66.

Tokunaga, H., Arakawa, T., and Tokunaga, M. (2014). Cys139Ser mutation in dimeric nucleoside diphosphate kinase generates catalytically competent monomer. Int. J. Biol Macromol. 66, 66-73.

Inoue, N., Takai, E., Arakawa, T., and Shiraki, K. (2014). Arginine and lysine reduce the high viscosity of serum albumin solutions for pharmaceutical injection. J. Biosci. Bioeng. 117, 539-543.

Ohtake, S. and Arakawa, T. (2013). Recombinant therapeutic protein vaccines. Protein Pept. Lett. 20, 1324-1344.

Ohtake, S., Kita, Y., Payne, R., Manning, M., and Arakawa, T. (2013). Structural characteristics of short peptides in solution. Protein Pept. Lett. 20, 1308-1323.

Tokunaga, Y., Matsumoto, M., Tokunaga, M., Arakawa, T., and Sugimoto, Y. (2013). Amyloid fibril formation in vitro from halophilic metal binding protein: its high solubility and reversibility minimized formation of amorphous protein aggregations. Protein Sci. 22, 1582-1591.

Takai, E., Yoshizawa, S., Ejima, D., Arakawa, T., and Shiraki, K. (2013). Synergistic solubilization of porcine myosin in physiological salt solution by arginine. Int. J. Biol. Macromol. 62, 647-651.

Tokunaga, H., Arakawa, T., and Tokunaga, M. (2013). Surface acidic amino acid of pseudomonas/halomonas chimeric nucleoside diphosphate kinase leads to effective recovery from heat- denaturation. Protein Pept. Lett. 20, 836-841.

Hirano, A., Kameda, T., Shinozaki, D., Arakawa, T., and Shiraki, K. (2013). Molecular dynamics simulation of the arginine-assisted solubilization of caffeic acid: intervention in the interaction. J. Phys. Chem. B 117, 7518-7527.

Onishi, H., Mizukami, M., Hanagata, H., Tokunaga, M., Arakawa, T., and Miyauchi, A. (2013). Efficient production of anti-fluorescein and anti-lysozyme as single-chain anti-body fragments (scFv) by Brevibacillus expression system. Protein Expr. Purif. 91, 184-191.

Shikiya, Y., Tomita, S., Arakawa, T., and Shiraki, K. (2013). Arginine inhibits adsorption of proteins on polystyrene surface. PLoS One 8, e70762

Tokunaga, M., Mizukami, M., Yamasaki, K., Tokunaga, H., Onishi, H., Hanagata, H., Ishibashi, M., Miyauchi, A., Tsumoto, K., and Arakawa, T. (2013). Secretory production of single-chain antibody (scFv) in Brevibacillus choshinensis using novel fusion partner. Appl. Microbiol. Biotechnol. 97, 8569-8580.

Yamaguchi, R., Ishibashi, M., Tokunaga, H., Arakawa, T., and Tokunaga, M. (2013). Structure of starch binding domains of halophilic alpha-amylase at low pH. Protein Pept. Lett. 20, 755-760.

Tokunaga, H., Furukawa, M., Arakawa, T., and Tokunaga, M. (2013). Channel forming outer membrane porin protein in halophile: expressed as a soluble form in Escherichia coli. Int. J. Biol Macromol. 54, 44-50.

Arakawa, T., Tokunaga, H., Ishibashi, M., and Tokunaga, M. (2012). Halophilic Properties and their Manipulation and Application. In: Extremophiles: Sustainable Resources and Biotechnological Implications. O.V.Singh, ed. John Wiley & Sons, Inc., Hoboken, N.J., pp. 95-121.

Yoshikawa, H., Hirano, A., Arakawa, T., and Shiraki, K. (2012). Mechanistic insights into protein precipitation by alcohol. Int. J. Biol. Macromol. 50, 865-871.

Ishibashi, M., Uchino, M., Arai, S., Kuroki, R., Arakawa, T., and Tokunaga, M. (2012). Reduction of salt-requirement of halophilic nucleoside diphosphate kinase by engineering S-S bond. Arch. Biochem. Biophys. 525, 47-52.

Yamaguchi, R., Arakawa, T., Tokunaga, H., Ishibashi, M., and Tokunaga, M. (2012). Effects of salt and ligand concentrations on the thermal unfolding and refolding of halophilic starch-binding domain from Kocuria varians alpha-amylase. Protein Pept. Lett. 19, 326-332.

Yamaguchi, R., Arakawa, T., Tokunaga, H., Ishibashi, M., and Tokunaga, M. (2012). Distinct characteristics of single starch-binding domain SBD1 derived from tandem domains SBD1-SBD2 of halophilic Kocuria varians alpha-amylase. Protein J. 31, 250-258.

Ikeda, K., Yamasaki, H., Minami, S., Suzuki, Y., Tsujimoto, K., Sekino, Y., Irie, H., Arakawa, T., and Koyama, A. H. (2012). Arginine inactivates human herpesvirus 2 and inhibits genital herpesvirus infection. Int. J. Mol Med. 30, 1307-1312.

Yamaguchi, R., Arakawa, T., Tokunaga, H., Ishibashi, M., and Tokunaga, M. (2012). Halophilic properties of metal binding protein characterized by high histidine content from Chromohalobacter salexigens DSM3043. Protein J. 31, 175-183.

Yoshikawa, H., Hirano, A., Arakawa, T., and Shiraki, K. (2012). Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin. Int.. J. Biol. Macromol. 50, 1286-1291.

Yamaguchi, R., Arakawa, T., Tokunaga, H., Ishibashi, M., and Tokunaga, M. (2012). Distinct characteristics of single starch-binding domain SBD1 derived from tandem domains SBD1-SBD2 of halophilic Kocuria varians alpha-amylase. Protein J. 31, 250-258.

Ariki, R., Hirano, A., Arakawa, T., and Shiraki, K. (2012). Drug solubilization effect of lauroyl-L-glutamate. J Biochem. 151, 27-33.

Hirano, A., Shiraki, K., and Arakawa, T. (2012). Polyethylene glycol behaves like weak organic solvent. Biopolymers 97, 117-122.

Ohtake, S., Kita, Y., and Arakawa, T. (2011). Interactions of formulation excipients with proteins in solution and in the dried state. Adv. Drug Deliv. Rev. 63, 1053-1073.

Arakawa, T., Niikura, T., and Kita, Y. (2011). The biological activity of Humanin analogs correlates with structure stabilities in solution. Int. J. Biol. Macromol. 49, 93-97.

Ishibashi, M., Ida, K., Tatsuda, S., Arakawa, T., and Tokunaga, M. (2011). Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase. Int. J. Biol. Macromol. 49, 778-783.

Ariki, R., Hirano, A., Arakawa, T., and Shiraki, K. (2011). Arginine increases the solubility of alkyl gallates through interaction with the aromatic ring. J. Biochem. 149, 389-394.

Misono, K. S., Philo, J. S., Arakawa, T., Ogata, C. M., Qiu, Y., Ogawa, H., and Young, H. S. (2011). Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase. FEBS J. 278, 1818-1829.

Arakawa, T., Hirano, A., Shiraki, K., Niikura, T., and Kita, Y. (2011). Advances in characterization of neuroprotective peptide, humanin. Curr. Med. Chem. 18, 5554-5563.

Rajan, R. S., Tsumoto, K., Tokunaga, M., Tokunaga, H., Kita, Y., and Arakawa, T. (2011). Chemical and pharmacological chaperones: application for recombinant protein production and protein folding diseases. Curr. Med. Chem. 18, 1-15.

Hirano, A., Shiraki, K., Niikura, T., Arakawa, T., and Kita, Y. (2011). Structure of three Humanin peptides with different activities upon interaction with liposome. Int. J. Biol. Macromol. 48, 360-363.

Ishibashi, M., Oda, K., Arakawa, T., and Tokunaga, M. (2011). Cloning, expression, purification and activation by Na ion of halophilic alkaline phosphatase from moderate halophile Halomonas sp. 593. Protein Expr. Purif. 76, 97-102.

Kudou, M., Yumioka, R., Ejima, D., Arakawa, T., and Tsumoto, K. (2011). A novel protein refolding system using lauroyl-l-glutamate as a solubilizing detergent and arginine as a folding assisting agent. Protein Expr. Purif. 75, 46-54.

Yamaguchi, R., Tokunaga, H., Ishibashi, M., Arakawa, T., and Tokunaga, M. (2011). Salt-dependent thermo-reversible alpha-amylase: cloning and characterization of halophilic alpha-amylase from moderately halophilic bacterium, Kocuria varians. Appl. Microbiol. Biotechnol. 89, 673-684.

Nishide, M., Tsujimoto, K., Uozaki, M., Ikeda, K., Yamasaki, H., Koyama, A. H., and Arakawa, T. (2011). Effects of electrolytes on virus inactivation by acidic solutions. Int. J. Mol. Med. 27, 803-809.

Qian, X., Mester, T., Morgado, L., Arakawa, T., Sharma, M. L., Inoue, K., Joseph, C., Salgueiro, C. A., Maroney, M. J., and Lovley, D. R. (2011). Biochemical characterization of purified OmcS, a c-type cytochrome required for insoluble Fe(III) reduction in Geobacter sulfurreducens. Biochim. Biophys. Acta 1807, 404-412.

Yamasaki, H., Tsujimoto, K., Ikeda, K., Suzuki, Y., Arakawa, T., and Koyama, A. H. (2011). Antiviral and virucidal activities of nalpha-cocoyl-L-arginine ethyl ester. Adv. Virol. 2011, 572868

Arakawa, T., Uozaki, M., and Hajime, K. A. (2010). Modulation of small molecule solubility and protein binding by arginine. Mol. Med. Report 3, 833-836.

Shiraki, K., Hirano, A., Kita, Y., Koyama, A. H., and Arakawa, T. (2010). Potential application of arginine in interaction analysis. Drug Discov. Ther. 4, 326-333.

Hirano, A., Kameda, T., Arakawa, T., and Shiraki, K. (2010). Arginine-assisted solubilization system for drug substances: solubility experiment and simulation. J. Phys. Chem. B 114, 13455-13462.

Arakawa, T. (2010). [Role of arginine in development of biopharmaceuticals]. Yakugaku Zasshi 130, 793-800.

Arakawa, T. (2010). Expression and refolding technologies for production of recombinant proteins. Curr. Pharm. Biotechnol. 11, 231-232.

Ohtake, S., Arakawa, T., and Koyama, A. H. (2010). Arginine as a synergistic virucidal agent. Molecules 15, 1408-1424.

Tsumoto, K., Arakawa, T., and Chen, L. (2010). Step-wise refolding of recombinant proteins. Curr. Pharm. Biotechnol. 11, 285-288.

Ikeda, K., Yamasaki, H., Suzuki, Y., Koyama, A. H., and Arakawa, T. (2010). Novel strategy with acidic arginine solution for the treatment of influenza A virus infection. Exp. Ther. Med. 1, 251-256.

Tsumoto, K., Abe, R., Ejima, D., and Arakawa, T. (2010). Non-denaturing solubilization of inclusion bodies. Curr. Pharm. Biotechnol. 11, 309-312.

Tsujimoto, K., Uozaki, M., Ikeda, K., Yamazaki, H., Utsunomiya, H., Ichinose, M., Koyama, A. H., and Arakawa, T. (2010). Solvent-induced virus inactivation by acidic arginine solution. Int. J Mol Med. 25, 433-437.

Arakawa, T., Ejima, D., Li, T., and Philo, J. S. (2010). The critical role of mobile phase composition in size exclusion chromatography of protein pharmaceuticals. J. Pharm. Sci. 99, 1674-1692.

Arakawa, T., Tokunaga, H., Yamaguchi, R., and Tokunaga, M. (2010). High solubility supports efficient refolding of thermally unfolded beta-lactamase. Int. J. Biol. Macromol. 47, 706-709.

Hirano, A., Shiraki, K., Niikura, T., Arakawa, T., and Kita, Y. (2010). Structure changes of natively disordered Humanin in the presence of lipid. Int. J. Biol. Macromol. 46, 375-379.

Arakawa, T., Futatsumori-Sugai, M., Tsumoto, K., Kita, Y., Sato, H., and Ejima, D. (2010). MEP HyperCel chromatography II: binding, washing and elution. Protein Expr. Purif. 71, 168-173.

Ogawa, H., Qiu, Y., Philo, J. S., Arakawa, T., Ogata, C. M., and Misono, K. S. (2010). Reversibly bound chloride in the atrial natriuretic peptide receptor hormone-binding domain: Possible allosteric regulation and a conserved structural motif for the chloride-binding site. Protein Sci. 19, 544-557.

Tokunaga, H., Arakawa, T., and Tokunaga, M. (2010). Novel soluble expression technologies derived from unique properties of halophilic proteins. Appl. Microbiol. Biotechnol. 88, 1223-1231.

Hirano, A., Tokunaga, H., Tokunaga, M., Arakawa, T., and Shiraki, K. (2010). The solubility of nucleobases in aqueous arginine solutions. Arch Biochem. Biophys. 497, 90-96.

Tokunaga, M., Arakawa, T., and Tokunaga, H. (2010). Recombinant expression in moderate halophiles. Curr. Pharm. Biotechnol. 11, 259-266.

Arakawa, T., Hirano, A., Shiraki, K., Kita, Y., and Koyama, A. H. (2010). Stabilizing and destabilizing effects of arginine on deoxyribonucleic acid. Int. J Biol Macromol. 46, 217-222.

Tokunaga, H., Saito, S., Sakai, K., Yamaguchi, R., Katsuyama, I., Arakawa, T., Onozaki, K., Arakawa, T., and Tokunaga, M. (2010). Halophilic beta-lactamase as a new solubility- and folding-enhancing tag protein: production of native human interleukin 1alpha and human neutrophil alpha-defensin. Appl. Microbiol. Biotechnol. 86, 649-658.

Yumioka, R., Tsumoto, K., Arakawa, T., and Ejima, D. (2010). Screening of effective column rinse solvent for Protein-A chromatography. Protein Express Purif. 70, 218-223.

Tokunaga, H., Izutsu, K. I., Arai, S., Yonezawa, Y., Kuroki, R., Arakawa, T., and Tokunaga, M. (2010). Dimer–tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacterium Chromohalobacter salexigens DSM3043: Both residues 134 and 136 are critical for the tetramer assembly. Enzyme and Microbial Technology 46, 129-136.

Arakawa, T., Futatsumori-Sugai, M., Tsumoto, K., Kita, Y., Sato, H., and Ejima, D. (2010). MEP HyperCel chromatography II: binding, washing and elution. Protein Expr. Purif. 71, 168-173.

Gagnon, P. and Arakawa, T. (2009). Hot topic: Aggregation detection and removal in biopharmaceutical proteins (editorial). Curr. Pharm. Biotechnol. 10, 337-347.

Philo, J. S. and Arakawa, T. (2009). Mechanisms of protein aggregation. Curr. Pharm. Biotechnol. 10, 348-351.

Hamada, H., Arakawa, T., and Shiraki, K. (2009). Effect of additives on protein aggregation. Curr. Pharm. Biotechnol. 10, 400-407.

Nakakido, M., Kudou, M., Arakawa, T., and Tsumoto, K. (2009). To be excluded or to bind, that is the question: Arginine effects on proteins. Curr. Pharm. Biotechnol. 10, 415-420.

Arakawa, T., Kita, Y., Sato, H., and Ejima, D. (2009). Stress-free chromatography: affinity chromatography. Curr. Pharm. Biotechnol. 10, 456-460.

Arakawa, T., Kita, Y., and Ejima, D. (2009). Stress-free chromatography: IEC and HIC. Curr. Pharm. Biotechnol. 10, 461-463.

Arakawa, T., Niikura, T., Kita, Y., and Arisaka, F. (2009). Structure analysis of short peptides by analytical ultracentrifugation: Review. Drug Discov. Ther. 3, 208-214.

Costantino, H. R., Culley, H., Chen, L., Morris, D., Houston, M., Roth, S., Phoenix, M. J., Foerder, C., Philo, J. S., Arakawa, T., Eidenschink, L., Andersen, N. H., Brandt, G., and Quay, S. C. (2009). Development of Calcitonin Salmon Nasal Spray: Similarity of peptide formulated in chlorobutanol compared to benzalkonium chloride as preservative. J. Pharm. Sci. 98, 3691-3706.

Futatsumori-Sugai, M., Abe, R., Watanabe, M., Kudou, M., Yamamoto, T., Ejima, D., Arakawa, T., and Tsumoto, K. (2009). Utilization of Arg-elution method for FLAG-tag based chromatography. Protein Express Purif. 67, 148-155.

Arakawa, T., Niikura, T., Arisaka, F., and Kita, Y. (2009). Short neuroprotective peptides, ADNF9 and NAP, are structurally disordered and monomeric in PBS. Int. J Biol Macromol. 45, 8-11.

Tokunaga, M., Tokunaga, H., Ishibashi, M., and Arakawa, T. (2009). [Halophilic enzymes: negative charges determine halophilicity]. Seikagaku 81, 401-406.

Senczuk, A. M., Klinke, R., Arakawa, T., Vedantham, G., and Yigzaw, Y. (2009). Hydrophobic interaction chromatography in dual salt system increases protein binding capacity. Biotechnol. Bioeng. 103, 930-935.

Ishibashi, M., Iwasa, T., Kumeda, K., Arakawa, T., and Tokunaga, M. (2009). Effects of mutations at Gly114 on the stability and refolding of haloarchaeal nucleoside diphosphate kinase in low salt solution. Int. J. Biol. Macromol. 44, 361-364.

Naito, T., Irie, H., Tsujimoto, K., Ikeda, K., Arakawa, T., and Koyama, A. H. (2009). Antiviral effect of arginine against herpes simplex virus type 1. Int. J Mol Med. 23, 495-499.

Arisaka, F., Arakawa, T., Niikura, T., and Kita, Y. (2009). Active form of neuroprotective Humanin, HN, and inactive analog, S7A-HN, are monomeric and disordered in aqueous phosphate solution at pH 6.0; No correlation of solution structure with activity. Protein Pept. Lett. 16, 132-137.

Utsunomiya, H., Ichinose, M., Tsujimoto, K., Katsuyama, Y., Yamasaki, H., Koyama, A. H., Ejima, D., and Arakawa, T. (2009). Co-operative thermal inactivation of herpes simplex virus and influenza virus by arginine and NaCl. Int. J Pharm. 366, 99-102.

Abe, R., Kudou, M., Tanaka, Y., Arakawa, T., and Tsumoto, K. (2009). Immobilized metal affinity chromatography in the presence of arginine. Biochem. Biophys. Res. Commun. 381, 306-310.

Arakawa, T., Kita, Y., and Koyama, A. H. (2009). Synergistic virus inactivation effects of arginine. Biotechnol. J 4, 174-178.

Arakawa, T., Kita, Y., Sato, H., and Ejima, D. (2009). MEP chromatography of antibody and Fc-fusion protein using aqueous arginine solution. Protein Expr. Purif. 63, 158-163.

Arakawa, T., Yamasaki, H., Ikeda, K., Ejima, D., Naito, T., and Koyama, A. H. (2009). Antiviral and virucidal activities of natural products. Curr. Med. Chem. 16, 2485-2497.

Hirano, A., Arakawa, T., and Shiraki, K. (2008). Arginine increases the solubility of coumarin: Comparison with salting-in and salting-out additives. J. Biochem. 144, 363-369.

Nakakido, M., Tanaka, Y., Mitsuhori, M., Kudou, M., Ejima, D., Arakawa, T., and Tsumoto, K. (2008). Structure-based analysis reveals hydration changes induced by arginine hydrochloride. Biophys. Chem. 137, 105-109.

Tokunaga, H., Arakawa, T., and Tokunaga, M. (2008). Engineering of halophilic enzymes: Two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases. Protein Sci. 17, 1603-1610.

Katsuyama, Y., Yamasaki, H., Tsujimoto, K., Koyama, A. H., Ejima, D., and Arakawa, T. (2008). Butyroyl-arginine as a potent virus inactivation agent. Int. J. Pharm. 361, 92-98.

Kita, Y., Niikura, T., Arisaka, F., and Arakawa, T. (2008). The complex structure transition of Humanin peptides by sodium dodecylsulfate and trifluoroethanol. Protein Pept. Lett. 15, 510-515.

Arakawa, T., Kita, Y., and Koyama, A. H. (2008). Solubility enhancement of gluten and organic compounds by arginine. Int. J. Pharm. 355, 220-223.

Arakawa, T., Kita, Y., Ejima, D., and Gagnon, P. (2008). Solvent modulation of column chromatography. Protein Pept. Lett. 15, 544-555.

Arakawa, T., Kita, Y., and Niikura, T. (2008). A rescue factor for Alzheimer's diseases: discovery, activity, structure, and mechanism. Curr. Med. Chem. 15, 2086-2098.

Arisaka, F., Niikura, T., Arakawa, T., and Kita, Y. (2008). The structure analysis of Humanin analog, AGA-(C8R)HNG17, by circular dichroism and sedimentation equilibrium: Comparison with the parent molecule. Int. J. Biol. Macromol. 43, 88-93.

Furuya, A., Uozaki, M., Yamasaki, H., Arakawa, T., Arita, M., and Koyama, A. H. (2008). Antiviral effects of ascorbic and dehydroascorbic acids in vitro. Int. J. Mol. Med. 22, 541-545.

Tokunaga, H., Ishibashi, M., Arisaka, F., Arai, S., Kuroki, R., Arakawa, T., and Tokunaga, M. (2008). Residue 134 determines the dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacteria. FEBS Lett. 582, 1049-1054.

Arakawa, T., Niikura, T., Arisaka, F., and Kita, Y. (2008). Activity-dependent neurotrophic factor, ADNF, determines the structure characteristics of Colivelin, a fusion protein of ADNF9 and Humanin analog. J. Pept. Sci. 14, 631-636.

Arakawa, T., Tsumoto, K., Kita, Y., Chang, B., and Ejima, D. (2007). Biotechnology applications of amino acids in protein purification and formulations. Amino Acids 33, 587-605.

Arakawa, T., Kita, Y., and Timasheff, S. N. (2007). Protein precipitation and denaturation by dimethyl sulfoxide. Biophys. Chem. 131, 62-70.

Arakawa, T., Philo, J. S., Ejima, D., Sato, H., and Tsumoto, K. (2007). Aggregation analysis of therapeutic proteins, part 3: Principles and optimization of field-flow fractionation (FFF). Bioprocess International 5 (10), 52-70. [PDF]

Arakawa, T., Takako, N., Hirohisa, T., Arisaka, F., and Kita, Y. (2007). Structure analysis of activity-dependent neurotrophic factor 9 by circular dichroism and sedimentation equilibrium. J. Mol. Neurosci. 33, 262-267.

Arakawa, T., Ejima, D., Tsumoto, K., Obeyama, N., Tanaka, Y., Kita, Y., and Timasheff, S. N. (2007). Suppression of protein interactions by arginine: A proposed mechanism of the arginine effects. Biophys. Chem. 127, 1-8.

Ishibashi, M., Tatsuda, S., Izutsu, K. I., Kumeda, K., Arakawa, T., and Tokunaga, M. (2007). A single Gly 114Arg mutation stabilizes the hexameric subunit assembly and changes the substrate specificity of halo-archaeal nucleoside diphosphate kinase. FEBS Lett. 581, 4073-4079.

Arakawa, T., Ejima, D., Tsumoto, K., Ishibashi, M., and Tokunaga, M. (2007). Improved performance of column chromatography by arginine: Dye-affinity chromatography. Protein Express Purif. 52, 410-414.

Heavner, G. A., Arakawa, T., Philo, J. S., Calmann, M. A., and Labrenz, S. (2007). Protein isolated from biopharmaceutical formulations cannot be used for comparative studies: Follow-up to "a case study using Epoetin Alfa from Epogen and EPREX". J. Pharm. Sci. 96, 3214-3225.

Tsumoto, K., Ejima, D., Nagase, K., and Arakawa, T. (2007). Arginine improves protein elution in hydrophobic interaction chromatography - The cases of human interleukin-6 and activin-A. J. Chromatogr. A 1154, 81-86.

Arakawa, T., Philo, J. S., Ejima, D., Tsumoto, K., and Arisaka, F. (2007). Aggregation analysis of therapeutic proteins, part 2: Analytical ultracentrifugation and dynamic light scattering. Bioprocess International 5 (4), 36-47. [PDF]

Arakawa, T., Tsumoto, K., Ejima, D., Kita, Y., Yonezawa, Y., and Tokunaga, M. (2007). Induced binding of proteins by ammonium sulfate in affinity and ion-exchange column chromatography. J. Biochem. Biophys. Meth. 70, 493-498.

Yamasaki, H., Uozaki, M., Katsuyama, Y., Utsunomiya, H., Arakawa, T., Higuchi, M., Higuti, T., and Koyama, A. H. (2007). Antiviral effect of octyl gallate against influenza and other RNA viruses. Int. J. Mol. Med. 19, 685-688.

Tsumoto, K., Ejima, D., Senczuk, A. M., Kita, Y., and Arakawa, T. (2007). Effects of salts on protein-surface interactions: applications for column chromatography. J. Pharm Sci. 96, 1677-1690.

Ejima, D., Tsumoto, K., and Arakawa, T. (2007). Improved column chromatography performance using arginine. Amer. Biotech. Lab. 25, 16-18.

Arakawa, T., Tsurnoto, K., Nagase, K., and Ejima, D. (2007). The effects of arginine on protein binding and elution in hydrophobic interaction and ion-exchange chromatography. Protein Express Purif. 54, 110-116.

Ejima, D., Tsumoto, K., Fukada, H., Yumioka, R., Nagase, K., Arakawa, T., and Philo, J. S. (2007). Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies. Proteins 66, 954-962.

Hsu, E., Osslund, T., Nybo, R., Chen, B. L., Kenney, W. C., Morris, C. F., Arakawa, T., and Narhi, L. O. (2006). Enhanced stability of recombinant keratinocyte growth factor by mutagenesis. Protein Eng. 19, 147-153.

Tokunaga, H., Arakawa, T., Fukada, H., and Tokunaga, M. (2006). Opposing effects of NaCl on reversibility and thermal stability of halophilic beta-lactamase from a moderate halophile, Chromohalobacter sp. 560. Biophys. Chem. 119, 316-320.

Arakawa, T., Ejima, D., Kita, Y., and Tsumoto, K. (2006). Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs. Biochim. Biophys. Acta 1764, 1677-1687.

Tokunaga, H., Oda, Y., Yonezawa, Y., Arakawa, T., and Tokunaga, M. (2006). Contribution of halophilic nucleoside diphosphate kinase sequence to the heat stability of chimeric molecule. Protein Pept. Lett. 13, 525-530.

Arakawa, T., Philo, J. S., Ejima, D., Tsumoto, K., and Arisaka, F. (2006). Aggregation analysis of therapeutic proteins, part 1: General aspects and techniques for assessment. Bioprocess International 4 (10), 42-49. [PDF]

Ejima, D., Ono, K., Tsumoto, K., Arakawa, T., and Eto, Y. (2006). A novel "reverse screening" to identify refolding additives for activin-A. Protein Expr. Purif. 47, 45-51.

Tokunaga, M., Arakawa, T., Ishibashi, M., and Tokunaga, H. (2005). [Familiar extremophiles, halophiles, and halophilic enzymes]. Seikagaku 77, 320-331.

Tsumoto, K., Ejima, D., Kita, Y., and Arakawa, T. (2005). Review: Why is arginine effective in suppressing aggregation? Protein Pept. Lett. 12, 613-619.

Arakawa, T., Niikura, T., Tajima, H., and Kita, Y. (2006). The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism. J. Pept. Sci. 12, 639-642.

Arakawa, T., Kita, Y., Ejima, D., Tsumoto, K., and Fukada, H. (2006). Aggregation suppression of proteins by arginine during thermal unfolding. Protein Pept. Lett. 13, 921-927.

Ishibashi, M., Tsumoto, K., Ejima, D., Arakawa, T., and Tokunaga, M. (2005). Characterization of arginine as a solvent additive: a halophilic enzyme as a model protein. Protein Pept. Lett. 12, 649-653.

Ishibashi, M., Tsumoto, K., Tokunaga, M., Ejima, D., Kita, Y., and Arakawa, T. (2005). Is arginine a protein-denaturant? Protein Expr. Purif. 42, 1-6.

Ejima, D., Yumioka, R., Arakawa, T., and Tsumoto, K. (2005). Arginine as an effective additive in gel permeation chromatography. J. Chromatogr. A 1094, 49-55.

Umetsu, M., Tsumoto, K., Nitta, S., Adschiri, T., Ejima, D., Arakawa, T., and Kumagai, I. (2005). Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by L-arginine. Biochem. Biophys Res. Commun. 328, 189-197.

Ejima, D., Yumioka, R., Tsumoto, K., and Arakawa, T. (2005). Effective elution of antibodies by arginine and arginine derivatives in affinity column chromatography. Anal. Biochem. 345, 250-257.

Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., Philo, J. S., and Arakawa, T. (2004). Role of arginine in protein refolding, solubilization, and purification. Biotechnol. Prog. 20, 1301-1308.

Ishibashi, M., Arakawa, T., and Tokunaga, M. (2004). Facilitated folding and subunit assembly in Escherichia coli and in vitro of nucleoside diphosphate kinase from extremely halophilic archaeon conferred by amino-terminal extension containing hexa-His-tag. FEBS Lett. 570, 87-92.

Tanaka, Y., Tsumoto, K., Umetsu, M., Nakanishi, T., Yasutake, Y., Sakai, N., Yao, M., Tanaka, I., Arakawa, T., and Kumagai, I. (2004). Structural evidence for guanidine-protein side chain interactions: crystal structure of CutA from Pyrococcus horikoshii in 3 M guanidine hydrochloride. Biochem. Biophys Res. Commun. 323, 185-191.

French, D. L., Arakawa, T., and Li, T. S. (2004). Fourier transformed infrared spectroscopic investigation of protein conformation in spray-dried protein/trehalose powders. Biopolymers 73, 524-531.

Arakawa, T., Philo, J. S., Tsumoto, K., Yumioka, R., and Ejima, D. (2004). Elution of antibodies from a Protein-A column by aqueous arginine solutions. Protein Expr. Purif. 36, 244-248.

Tokunaga, H., Ishibashi, M., Arakawa, T., and Tokunaga, M. (2004). Highly efficient renaturation of β-lactamase isolated from moderately halophilic bacteria. FEBS Lett. 558, 7-12.

Arakawa, T., Katsuyama, I., Kumagai, I., and Tsumoto, K. (2003). [A magic agent in protein refolding: arginine]. Tanpakushitsu Kakusan Koso 48, 2310-2317.

Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., and Arakawa, T. (2003). Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem. Biophys. Res. Commun. 312, 1383-1386.

Tsumoto, K., Ejima, D., Kumagai, I., and Arakawa, T. (2003). Practical considerations in refolding proteins from inclusion bodies. Protein Expr. Purif. 28, 1-8.

Ishibashi, M., Sakashita, K., Tokunaga, H., Arakawa, T., and Tokunaga, M. (2003). Activation of halophilic nucleoside diphosphate kinase by a non-ionic osmolyte, trimethylamine N-oxide. J. Protein Chem. 22, 345-351.

Yokoyama, K., Ohtsuka, K., Kuraishi, C., Ono, K., Kita, Y., Arakawa, T., and Ejima, D. (2003). Gelation of food protein induced by recombinant microbial transglutaminase. Journal of Food Science 68, 48-51.

Arakawa, T. and Tsumoto, K. (2003). The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304, 148-152.

Yokoyama, K., Ejima, D., Kita, Y., Philo, J. S., and Arakawa, T. (2003). Structure of folding intermediates at pH 4.0 and native state of microbial transglutaminase. Biosci. Biotechnol. Biochem. 67, 291-294.

Arakawa, T. and Philo, J. S. (2002). Biophysical and biochemical analysis of recombinant proteins. In: Pharmaceutical Biotechnology, 2nd edition. D. J .A. Crommelin and R. D. Sindelar, eds. Taylor & Francis, London, pp. 25-51.

Ishibashi, M., Arakawa, T., Philo, J.S., Sakashita, K., Yonezawa, Y., Tokunaga, H., and Tokunaga, M. (2002) Secondary and quaternary structural transition of the halophilic archaeon nucleoside diphosphate kinase under high- and low-salt conditions. FEMS Microbiol. Lett. 216, 235-241.

Arakawa, T., Li, T., and Narhi, L. O. (2002). Recombinant production of native proteins from Escherichia coli. Pharm. Biotechnol. 13, 27-60.

Toyoda, T., Arakawa, T., and Yamaguchi, H. (2002). N-glycans stabilize human erythropoietin through hydrophobic interactions with the hydrophobic protein surface: studies by surface plasmon resonance analysis. J. Biochem. (Tokyo) 131, 511-515.

Kita, Y. and Arakawa, T. (2002). Salts and glycine increase reversibility and decrease aggregation during thermal unfolding of ribonuclease-A. Biosci. Biotechnol. Biochem. 66, 880-882.

Li, T. S., Talvenheimo, J., Zeni, L., Rosenfeld, R., Stearns, G., and Arakawa, T. (2002). Changes in protein conformation and dynamics upon complex formation of brain-derived neurotrophic factor and its receptor: Investigation by isotope-edited Fourier transform IR spectroscopy. Biopolymers 67, 10-19.

Li, T., Yamane, H., Arakawa, T., Narhi, L. O., and Philo, J. (2002). Effect of the intermolecular disulfide bond on the conformation and stability of glial cell line-derived neurotrophic factor. Protein Eng 15, 59-64.

Arakawa, T. and Wen, J. (2001). Determination of carbohydrate contents from excess light scattering. Anal. Biochem. 299, 158-161.

Tokunaga, M., Shiraishi, Y., Odachi, M., Mizukami, M., Tokunaga, H., Philo, J. S., Arakawa, T., Ishibashi, M., Tanaka, R., and Takagi, H. (2001). Molecular cloning of groESL locus, and purification and characterization of chaperonins, GroEL and GroES, from Bacillus brevis. Biosci. Biotechnol. Biochem. 65, 1379-1387.

Arakawa, T., Philo, J. S., and Kita, Y. (2001). Kinetic and thermodynamic analysis of thermal unfolding of recombinant erythropoietin. Biosci. Biotechnol. Biochem. 65, 1321-1327.

Wen, J., Zhang, M., Horan, T.P., Philo, J.S., Li, T.S., Wypych, J., Mendiaz, E.A., Langley, K.E., Aoki, K.H., Kuwamoto, M., Kita, Y., and Arakawa, T. (2001). Copper staining method for extracting biologically active proteins from native gels. Biosci. Biotechnol. Biochem. 65, 1315-1320.

Narhi, L.O., Arakawa, T., Aoki, K., Wen, J., Elliott, S., Boone, T., and Cheetham, J. (2001). Asn to Lys mutations at three sites which are N-glycosylated in the mammalian protein decrease the aggregation of Escherichia coli-derived erythropoietin. Protein Eng. 14, 135-140.

Arakawa, T., Prestrelski, S.J., Kenney, W.C., and Carpenter, J.F. (2001). Factors affecting short-term and long-term stabilities of proteins. Adv. Drug Deliv. Rev. 46, 307-326.

Ishibashi, M., Tokunaga, H., Hiratsuka, K., Yonezawa, Y., Tsurumaru, H., Arakawa, T., and Tokunaga, M. (2001). NaCl-activated nucleoside diphosphate kinase from extremely halophilic archaeon, Halobacterium salinarum, maintains native conformation without salt. FEBS Lett. 493, 134-138.

Toyoda, T., Itai, T., Arakawa, T., Aoki, K.H., and Yamaguchi, H. (2000). Stabilization of human recombinant erythropoietin through interactions with the highly branched N-glycans. J. Biochem. (Tokyo) 128, 731-737.

Wato, S., Kamei, K., Arakawa, T., Philo, J.S., Wen, J., Hara, S., and Yamaguchi, H. (2000). A chimera-like alpha-amylase inhibitor suggesting the evolution of Phaseolus vulgaris alpha-amylase Inhibitor. J. Biochem. (Tokyo) 128, 139-144.

Arakawa, T. and Kita, Y. (2000). Stabilizing effects of caprylate and acetyltryptophanate on heat- induced aggregation of bovine serum albumin. Biochim. Biophys. Acta 1479, 32-36.

Arakawa, T. and Kita, Y. (2000). Protection of bovine serum albumin from aggregation by tween 80. J. Pharm. Sci. 89, 646-651.

Wen, J. and Arakawa, T. (2000). Refractive index of proteins in aqueous sodium chloride. Anal. Biochem. 280, 327-329.

Tokunaga, H., Hara, S., Arakawa, T., Ishibashi, M., Gupta, R.S., and Tokunaga, M. (1999). Identification and partial purification of DnaK homologue from extremely halophilic archaebacteria, Halobacterium cutirubrum. J. Protein Chem. 18, 837-844.

Arakawa, T. and Philo, J.S. (1999). [Applications of Analytical Ultracentrifuge to Molecular Biology and Pharmaceutical Science]. Yakugaku Zasshi 119, 597-611.

Arakawa, T. and Kita, Y. (1999). Refractive index of proteins in organic solvents. Anal. Biochem. 271, 119-120.

Caughey, D. J., Narhi, L. O., Kita, Y., Meng, S. Y., Wen, D., Chen, W., Ratzkin, B. J., Fujimoto, J., Iwahara, T., Yamamoto, T., and Arakawa, T. (1999). Fractionation of polyclonal antibodies to fragments of a neuroreceptor using three increasingly chaotropic solvents. J.Chromatogr.B Biomed.Sci.Appl. 728, 49-57.

Danilenko, D. N., Montestruque, S., Philo, J. S., Li, T. S., Hill, D., Speakman, J., Bahru, M., Zhang, M. S., Konishi, O., Itoh, N., Chirica, M., Delaney, J., Hernday, N., Martin, F., Hara, S., Talvenheimo, J., Narhi, L. O., and Arakawa, T. (1999). Recombinant rat fibroblast growth factor-16: Structure and biological activity. Arch. Biochem. Biophys. 361, 34-46.

Narhi, L. O., Philo, J. S., Sun, B., Chang, B. S., and Arakawa, T. (1999). Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor. Pharm. Res. 16, 799-807.

Haniu, M., Arakawa, T., Bures, E. J., Young, Y., Hui, J. O., Rohde, M. F., Welcher, A. A., and Horan, T. (1998). Human leptin receptor - Determination of disulfide structure and N-glycosylation sites of the extracellular domain. J. Biol. Chem. 273, 28691-28699.

Horan, T. P., Simonet, L., Jacobsen, R., Mann, M., Haniu, M., Wen, J., Arakawa, T., Kuwamoto, M., and Martin, F. (1998). Coexpression of G-CSF with an unglycosylated G-CSF receptor mutant results in secretion of a stable complex. Protein Expr. Purif. 14, 45-53.

Hu, M. C., Qiu, W. R., Wang, Y. P., Hill, D., Ring, B. D., Scully, S., Bolon, B., DeRose, M., Luethy, R., Simonet, W. S., Arakawa, T., and Danilenko, D. M. (1998). FGF-18, a novel member of the fibroblast growth factor family, stimulates hepatic and intestinal proliferation. Mole. Cell. 18, 6063-6074.

Koyama, A. H., Arakawa, T., and Adachi, A. (1998). Acceleration of virus-induced apoptosis by tumor necrosis factor. FEBS Letters 426, 179-182.

Li, T., Narhi, L. O., Wen, J., Philo, J. S., Sitney, K., Inoue, J., Yamamoto, T., and Arakawa, T. (1998). Interactions between NFkappaB and its inhibitor ikappaB: biophysical characterization of a NFkappaB/ikappaB-alpha complex. J. Prot. Chem. 17, 757-763.

Miyake, A., Konishi, M., Martin, F. H., Hernday, N. A., Ozaki, K., Yamamoto, S., Mikami, T., Arakawa, T., and Itoh, N. (1998). Structure and expression of a novel member, FGF-16, of the fibroblast growth factor family. Biochem. Biophys. Res. Commun. 243, 148-152.

Narhi, L. O., Wypych, J., Li, T., Langley, K. E., and Arakawa, T. (1998). Changes in conformation and stability upon SCF/sKit complex formation. J. Prot. Chem. 17 , 387-396.

Osslund, T. D., Syed, R., Singer, E., Hsu, E. W., Nybo, R., Chen, B. L., Harvey, T., Arakawa, T., Narhi, L. O., Chirino, A., and Morris, C. F. (1998). Correlation between the 1.6 A crystal structure and mutational analysis of keratinocyte growth factor. Protein Sci. 7, 1681-1690.

Takahashi, C., Sheng, Z., Horan, T. P., Kitayama, H., Maki, M., Hitomi, K., Kitaura, Y., Takai, S., Sasahara, R. M., Horimoto, A., Ikawa, Y., Ratzkin, B. J., Arakawa, T., and Noda, M. (1998). Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK. Proc.Natl.Acad.Sci.U.S.A 95, 13221-13226.

Tanaka, R., Tokunaga, H., Hara, S., Arakawa, T., and Tokunaga, M. (1998). Expression and purification of cytokine receptor homology domain of human granulocyte-colony stimulating factor receptor in Escherichia coli . Bioscience, Biotechnology and Biochemistry 62, 1809-1811.

Horan, T. P., Martin, F., Simonet, L., Arakawa, T., and Philo, J. S. (1997). Dimerization of granulocyte-colony stimulating factor receptor: the Ig plus CRH construct of granulocyte-colony stimulating factor receptor forms a 2:2 complex with a ligand. J. Biochem. (Tokyo) 121, 370-375.

Iwahara, T., Fujimoto, J., Wen, D., Cupples, R., Bucay, N., Arakawa, T., Mori, S., Ratzkin, B., and Yamamoto, T. (1997). Molecular characterization of ALK, a receptor tyrosine kinase expressed specifically in the nervous system. Oncogene 14, 439-449.

Kendrick, B. S., Chang, B. S., Arakawa, T., Peterson, B., Randolph, T. W., Manning, M. C., and Carpenter, J. F. (1997). Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: Role in restricted conformational mobility and compaction of native state. Proc. Natl. Acad. Sci. USA 94, 11917-11922.

Kendrick, B. S., Chang, B. S., Arakawa, T., Peterson, B., Randolph, T. W., Manning, M. C., and Carpenter, J. F. (1997). Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state. Proc.Natl.Acad.Sci.USA 94, 11917-11922.

Kolvenbach, C. G., Narhi, L. O., Philo, J. S., Li, T., Zhang, M., and Arakawa, T. (1997). Granulocyte-colony stimulating factor maintains a thermally stable, compact, partially folded structure at pH2. J.Pept.Res. 50, 310-318.

Li, T., Horan, T. P., Osslund, T., Stearns, G., and Arakawa, T. (1997). Conformational changes in G-CSF/Receptor complex as investigated by isotope-edited FTIR spectroscopy. Biochemistry 36, 8849-8857.

Liu, Y. W., Chen, B. K., Chen, C. J., Arakawa, T., Yoshimoto, T., Yamamoto, S., and Chang, W. C. (1997). Epidermal growth factor enhances transcription of human arachidonate 12- lipoxygenase in A431 cells. Biochim.Biophys.Acta 1344, 38-46.

Nakaguchi, T., Arakawa, T., Philo, J. S., Wen, J., Ishimoto, M., and Yamaguchi, H. (1997). Structural characterization of an a-amylase inhibitor from a wild common bean (Phaseolus vulgaris): Insight into the common structural features of leguminous a-amylase inhibitors. J. Biochem. (Tokyo) 121, 350-354.

Narhi, L. O., Caughey, D. J., Horan, T., Kita, Y., Chang, D., and Arakawa, T. (1997). Effect of three elution buffers on the recovery and structure of monoclonal antibodies. Anal. Biochem. 253, 236-245.

Narhi, L. O., Aoki, K. H., Philo, J. S., and Arakawa, T. (1997). Changes in conformation and stability upon formation of complexes of erythropoietin (EPO) and soluble EPO receptor. J. Prot. Chem. 16, 213-225.

Narhi, L. O., Caughey, D. J., Horan, T. P., Kita, Y., Chang, D., and Arakawa, T. (1997). Fractionation and characterization of polyclonal antibodies using three progressively more chaotropic solvents. Anal. Biochem. 253, 246-252.

Narhi, L. O., Rosenfeld, R., Shimamoto, G., Lee, R., Hawkins, N., Li, T., Philo, J. S., Wen, J., and Arakawa, T. (1997). Comparison of solution properties of human and rat ciliary neurotrophic factor. J.Pept.Res. 50, 300-309.

Rosenfeld, R. D., Miller, J. A., Narhi, L. O., Hawkins, N., Katta, V., Lauren, S., Weiss, M. A., and Arakawa, T. (1997). Putative folding pathway of insulin-like growth factor-I. Arch. Biochem. Biophys. 342, 298-305.

Wen, J., Arakawa, T., Wypych, J., Langley, K. E., Schwartz, M. G., and Philo, J. S. (1997). Chromatographic determination of extinction coefficients of non-glycosylated proteins using refractive index (RI) and UV absorbance (UV) detectors: Applications for studying protein interactions by size exclusion chromatography with light-scattering, UV, and RI detectors. In 'Techniques in Protein Chemistry VIII.' (Ed D. R. Marshak.) pp. 113-119. (Academic Press: San Diego.)

Arakawa, T., Li, T., Philo, J. S., Narhi, L. O., Horan, T. P., and Osslund, T. D. (1996). Characterization of granulocyte-colony stimulating factor: structure and interactions with its receptor. EOS J.Immunol.Immunopharmacol. 16, 35-40.

Chang, B. S., Beauvais, R. M., Arakawa, T., Narhi, L. O., Dong, A. C., Aparisio, D. I., and Carpenter, J. F. (1996). Formation of an active dimer during storage of interleukin-1 receptor antagonist in aqueous solution. Biophysical Journal 71, 3399-3406.

Chen, B. L. and Arakawa, T. (1996). Stabilization of recombinant human keratinocyte growth factor by osmolytes and salts. J. Pharm. Sci. 85, 419-422.

Haniu, M., Horan, T., Arakawa, T., Le, J., Katta, V., Hara, S., and Rohde, M. F. (1996). Disulfide structure and N-glycosylation sites of an extracellular domain of granulocyte-colony stimulating factor receptor. Biochemistry 35, 13040-13046.

Horan, T. P., Wen, J., Narhi, L. O., Parker, V., Garcia, A., Arakawa, T., and Philo, J. S. (1996). Dimerization of the extracellular domain of granulocyte-colony stimulating factor receptor by ligand binding: A monovalent ligand induces 2:2 complexes. Biochemistry 35, 4886-4896.

Hua, Q. X., Narhi, L. O., Jia, W., Arakawa, T., Rosenfeld, R., Hawkins, N., Miller, J. A., and Weiss, M. A. (1996). Native and non-native structure in a protein-folding intermediate: spectroscopic studies of partially reduced IGF-I and an engineered alanine model. Journal of Molecular Biology 259, 297-313.

Kasahara, K., Hayashi, K., Arakawa, T., Philo, J. S., Wen, J., Hara, S., and Yamaguchi, H. (1996). Complete sequence, subunit structure, and complexes with pancreatic alpha-amylase of an alpha-amylase inhibitor from Phaseolus vulgaris white kidney beans. J. Biochem. (Tokyo) 120, 177-183.

Kita, Y., Tseng, J., Horan, T. P., Wen, J., Philo, J. S., Chang, D., Ratzkin, B., Pacifici, R., Brankow, D., Hu, S., Luo, Y., Wen, D., Arakawa, T., and Nicolson, M. (1996). ErbB receptor activation, cell morphology changes, and apoptosis induced by anti-Her2 monoclonal antibodies. Biochem. Biophys. Res. Commun. 226, 59-69.

Narhi, L. O., Philo, J. S., Li, T. S., Zhang, M., Samal, B., and Arakawa, T. (1996). Induction of a-helix in the b-sheet protein tumor necrosis factor-a: Thermal- and trifluoroethanol-induced denaturation at neutral pH. Biochemistry 35, 11447-11453.

Narhi, L. O., Philo, J. S., Li, T. S., Zhang, M., Samal, B., and Arakawa, T. (1996). Induction of a-helix in the b-sheet protein tumor necrosis factor-a: Acid-induced denaturation. Biochemistry 35, 11454-11460.

Niven, R. W., Prestrelski, S. J., Treuheit, M. J., Ip, A. Y., and Arakawa, T. (1996). Protein nebulization. 2. Stabilization of G-CSF to air-jet nubulization and the role of protectants. Int.J.Pharm. 127, 191-201.

Philo, J. S., Aoki, K. H., Arakawa, T., Narhi, L. O., and Wen, J. (1996). Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one low-affinity interaction. Biochemistry 35, 1681-1691.

Samal, B., Boone, T., Karan, B., Chen, K., Sachdev, R., and Arakawa, T. (1996). Cloning and expression of the gene encoding a novel proteinase from Tritirachium album limber. Advances in Experimental Medicine and Biology 379, 95-104.

Wen, J., Arakawa, T., Talvenheimo, J., Welcher, A. A., Horan, T. P., Kita, Y. A., Tseng, J., Nicolson, M., and Philo, J. S. (1996). A light scattering/size exclusion chromatography method for studying the stoichiometry of a protein-protein complex. In 'Techniques in Protein Chemistry VII.' pp. 23-31. (Academic Press: San Diego)

Wen, J., Hsu, E., Kenney, W. C., Philo, J. S., Morris, C. F., and Arakawa, T. (1996). Characterization of keratinocyte growth factor binding to heparin and dextran sulfate. Arch. Biochem. Biophys. 332, 41-46.

Wen, J., Arakawa, T., and Philo, J. S. (1996). Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240, 155-166.

Zhang, M. Z., Pikal, K., Nguyen, T., Arakawa, T., and Prestrelski, S. J. (1996). The effect of the reconstitution medium on aggregation of lyophilized recombinant interleukin-2 and ribonuclease A. Pharm. Res. 13, 643-646.

Arakawa, T., Horan, T. P., Leong, K., Prestrelski, S. J., Narhi, L. O., and Hu, S. (1995). Structure and activity of granulocyte colony-stimulating factor derived from CHO cells containing cDNA coding for alternatively spliced sequences. Arch. Biochem. Biophys. 316, 285-289.

Arakawa, T., Holst, P., Narhi, L. O., Philo, J. S., Wen, J., Prestrelski, S. J., Zhu, X. T., Rees, D. C., and Fox, G. M. (1995). The importance of Arg40 and 45 in the mitogenic activity and structural stability of basic fibroblast growth factor: Effects of acidic amino acid substitutions. J. Prot. Chem. 14, 263-274.

Haniu, M., Horan, T., Arakawa, T., Le, J., Katta, V., and Rohde, M. F. (1995). Extracellular domain of granulocyte-colony stimulating factor receptor - Interaction with its ligand and identification of a domain in close proximity of ligand-binding region. Arch. Biochem. Biophys. 324, 344-356.

Horan, T. P., Wen, J., Arakawa, T., Liu, N., Brankow, D., Hu, S., Ratzkin, B., and Philo, J. S. (1995). Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. J. Biol. Chem. 270, 24604-24608.

Ip, A. Y., Arakawa, T., Silvers, H., Ransone, C. M., and Niven, R. W. (1995). Stability of recombinant consensus interferon to air-jet and ultrasonic nebulization. J. Pharm. Sci. 84, 1210-1214.

Murray, H. W., Hariprashad, J., Aguero, B., Arakawa, T., and Yeganegi, H. (1995). Antimicrobial response of a T cell-deficient host to cytokine therapy: effect of interferon-gamma in experimental visceral leishmaniasis in nude mice. J.Infect.Dis. 171, 1309-1316.

Niven, R. W., Ip, A. Y., Mittelman, S., Prestrelski, S. J., and Arakawa, T. (1995). Some factors associated with the ultrasonic nebulization of proteins. Pharm. Res. 12, 53-59.

Prestrelski, S. J., Pikal, K. A., and Arakawa, T. (1995). Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using fourier-transform infrared spectroscopy. Pharm. Res. 12, 1250-1259.

Samal, B. B., Arakawa, T., Boone, T. C., Jones, T., Prestrelski, S. J., Narhi, L. O., Wen, J., Stearns, G. W., Crandall, C. A., and Pope, J. (1995). High level expression of human leukemia inhibitory factor (LIF) from a synthetic gene in Escherichia coli and the physical and biological characterization of the protein. Biochim.Biophys.Acta 1260, 27-34.

Zhang, M. Z., Wen, J., Arakawa, T., and Prestrelski, S. J. (1995). A new strategy for enhancing the stability of lyophilized protein: The effect of the reconstitution medium on keratinocyte growth factor. Pharm. Res. 12, 1447-1452.

Arakawa, T., Philo, J. S., and Kenney, W. C. (1994). Structure and solubility of interleukin-2 in sodium dodecyl sulfate. International Journal of Peptide and Protein Research 43, 583-587.

Arakawa, T., Haniu, M., Narhi, L. O., Miller, J. A., Talvenheimo, J., Philo, J. S., Chute, H. T., Matheson, C., Carnahan, J., Louis, J.-C., Yan, Q., Welcher, A. A., and Rosenfeld, R. (1994). Formation of heterodimers from 3 neurotrophins, nerve growth- factor, neurotrophin-3, and brain-derived neurotrophic factor. J. Biol. Chem. 269, 27833-27839.

Arakawa, T., Wen, J., and Philo, J. S. (1994). Stoichiometry of heparin binding to basic fibroblast growth factor. Arch. Biochem. Biophys. 308, 267-273.

Chen, B. L., Arakawa, T., Morris, C. F., Kenney, W. C., Wells, C. M., and Pitt, C. G. (1994). Aggregation pathway of recombinant human keratinocyte growth factor and its stabilization. Pharm. Res. 11, 1581-1587.

Chen, B. L., Arakawa, T., Hsu, E., Narhi, L. O., Tressel, T. J., and Chien, S. L. (1994). Strategies to suppress aggregation of recombinant keratinocyte growth factor during liquid formulation development. J. Pharm. Sci. 83, 1657-1661.

Kenney, W. C., Haniu, M., Herman, A. C., Arakawa, T., Costigan, V. J., Lary, J., Yphantis, D. A., and Thomason, A. R. (1994). Formation of mitogenically active PDGF-B dimer does not require interchain disulfide bonds. J. Biol. Chem. 269, 12351-12359.

Kita, Y., Arakawa, T., Lin, T. Y., and Timasheff, S. N. (1994). Contribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry 33, 15178-15189.

Philo, J. S., Talvenheimo, J., Wen, J., Rosenfeld, R., Welcher, A. A., and Arakawa, T. (1994). Interactions of neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3/BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors. J. Biol. Chem. 269, 27840-27846.

Prestrelski, S. J., Arakawa, T., Duker, K., Kenney, W. C., and Narhi, L. O. (1994). The conformational stability of a non-covalent dimer of a platelet- derived growth factor-B mutant lacking the two cysteines involved in interchain disulfide bonds. International Journal of Peptide and Protein Research 44, 357-363.

Arakawa, T., Horan, T. P., Narhi, L. O., Rees, D. C., Schiffer, S. G., Holst, P. L., Prestrelski, S. J., Tsai, L. B., and Fox, G. M. (1993). Production and characterization of an analog of acidic fibroblast growth factor with enhanced stability and biological activity. Protein Eng. 6, 541-546.

Arakawa, T., Hung, L., Pan, V., Horan, T. P., Kolvenbach, C. G., and Narhi, L. O. (1993). Analysis of the heat-induced denaturation of proteins using temperature gradient gel electrophoresis. Anal. Biochem. 208, 255-259.

Arakawa, T., Prestrelski, S. J., Kenney, W. C., and Carpenter, J. F. (1993). Factors affecting short-term and long-term stabilities of proteins. Adv.Drug Deliv.Rev. 10, 1-28.

Arakawa, T., Wen, J., and Philo, J. S. (1993). Densimetric determination of equilibrium binding of sucrose octasulfate with basic fibroblast growth factor. J. Prot. Chem. 12, 689-693.

Arakawa, T., Prestrelski, S. J., Narhi, L. O., Boone, T. C., and Kenney, W. C. (1993). Cysteine 17 of recombinant human granulocyte-colony stimulating factor is partially solvent-exposed. J. Prot. Chem. 12, 525-532.

Carpenter, J. F., Prestrelski, S. J., and Arakawa, T. (1993). Separation of free. Arch. Biochem. Biophys. 303, 456-464.

Carpenter, J. F., Prestrelski, S. J., and Arakawa, T. (1993). Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization.  I. Enzyme activity and calorimetric studies. Arch. Biochem. Biophys. 303, 456-464.

Haniu, M., Narhi, L. O., Arakawa, T., Elliott, S., and Rohde, M. F. (1993). Recombinant human erythropoietin (rHuEPO): cross-linking with disuccinimidyl esters and identification of the interfacing domains in EPO. Protein Sci. 2, 1441-1451.

Hunt, P., Hokom, M. M., Hornkohl, A., Wiemann, B., Rohde, M. F., and Arakawa, T. (1993). The effect of the platelet-derived glycosaminoglycan serglycin on in vitro proplatelet-like process formation. Exp.Hematol. 21, 1295-1304.

Hunt, P., Hokom, M. M., Wiemann, B., Leven, R. M., and Arakawa, T. (1993). Megakaryocyte proplatelet-like process formation in vitro is inhibited by serum prothrombin, a process which is blocked by matrix-bound glycosaminoglycans. Exp.Hematol. 21, 372-381.

Kolvenbach, C. G., Elliott, S., Sachdev, R., Arakawa, T., and Narhi, L. O. (1993). Characterization of two fluorescent tryptophans in recombinant human granulocyte-colony stimulating factor: comparison of native sequence protein and tryptophan-deficient mutants. J. Prot. Chem. 12, 229-236.

Lauren, S. L., Arakawa, T., Stoney, K., and Rohde, M. F. (1993). Covalent dimerization of recombinant human interferon-gamma. Arch. Biochem. Biophys. 306, 350-353.

Miller, J. A., Narhi, L. O., Hua, Q. X., Rosenfeld, R., Arakawa, T., Rohde, M., Prestrelski, S., Lauren, S., Stoney, K. S., and Tsai, L. (1993). Oxidative refolding of insulin-like growth factor 1 yields two products of similar thermodynamic stability: a bifurcating protein-folding pathway. Biochemistry 32, 5203-5213.

Narhi, L. O., Kenney, W. C., Prestrelski, S. J., Arakawa, T., Lyons, D., Lary, J., and Yphantis, D. A. (1993). Conformation of glutathione adduct and oxidized forms of platelet- derived growth factor. International Journal of Peptide and Protein Research 41, 8-14.

Narhi, L. O., Rosenfeld, R., Wen, J., Arakawa, T., Prestrelski, S. J., and Philo, J. S. (1993). Acid-induced unfolding of brain-derived neurotrophic factor results in the formation of a monomeric "A state". Biochemistry 32, 10819-10825.

Narhi, L. O., Rosenfeld, R., Talvenheimo, J., Prestrelski, S. J., Arakawa, T., Lary, J. W., Kolvenbach, C. G., Hecht, R., Boone, T., Miller, J. A., and Yphantis, D. A. (1993). Comparison of the biophysical characteristics of human brain- derived neurotrophic factor, neurotrophin-3, and nerve growth factor. J. Biol. Chem. 268, 13309-13317.

Narhi, L. O., Hua, Q.-X., Arakawa, T., Fox, G. M., Tsai, L., Rosenfeld, R., Holst, P., Miller, J. A., and Weiss, M. A. (1993). Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: Genetic models of protein- folding intermediates. Biochemistry 32, 5214-5221.

Niewold, T. A., Gruys, E., Arakawa, T., Shirahama, T., and Kisilevsky, R. (1993). Recombinant human tumour necrosis factor-alpha (rhTNF-alpha) and rhTNF- alpha analogue enhance amyloid deposition in the Syrian hamster. Scand.J.Immunol. 37, 29-32.

Niewold, T. A., Arakawa, T., Kisilevsky, R., Shirahama, T., and Gruys, E. (1993). Human recombinant TNF-alpha and poly-I poly-C induce SAA and enhance amyloidosis in hamster. In 'Amyloid and amyloidosis, 1990; sixth international symposium on amyloidosis.' (Ed J. B. Natvig.) pp. 68-70. (Kluwer Academic Publishers: Norwell,MA.)

Philo, J. S., Rosenfeld, R., Arakawa, T., Wen, J., and Narhi, L. O. (1993). Refolding of brain-derived neurotrophic factor from guanidine hydrochloride:  Kinetic trapping in a collapsed form which is incompetent for dimerization. Biochemistry 32, 10812-10818.

Prestrelski, S. J., Arakawa, T., and Carpenter, J. F. (1993). Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization.  II. Structural studies using infrared spectroscopy. Arch. Biochem. Biophys. 303, 465-473.

Prestrelski, S. J., Tedeschi, N., Arakawa, T., and Carpenter, J. F. (1993). Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophysical Journal 65, 661-671.

Rosenfeld, R., Philo, J. S., Haniu, M., Stoney, K., Rohde, M. F., Wu, G.-M., Narhi, L. O., Wong, C., Boone, T., Hawkins, N. N., Miller, J. M., and Arakawa, T. (1993). Sites of iodination in recombinant human brain-derived neurotrophic factor and its effect on neurotrophic activity. Protein Science 2, 1664-1674.

Rosenfeld, R. D., Noone, N. M., Lauren, S. L., Rohde, M. F., Narhi, L. O., and Arakawa, T. (1993). Mutation of Arg55/56 to Leu55/Ala56 in insulin-like growth factor-I results in two forms different in disulfide structure and native conformation but similar under reverse-phase conditions. J. Prot. Chem. 12, 247-254.

Samal, B. B., Stearns, G. W., Boone, T. C., and Arakawa, T. (1993). Comparative analysis of the effects of recombinant cytokines on the growth and differentiation of ML-1, a human myelogenous leukemic cell line. Leuk.Res. 17, 299-304.

Arakawa, T. (1992). [Mechanism of stabilization of proteins by additives in freezing]. Tanpakushitsu Kakusan Koso 37, 1517-1524.

Arakawa, T., Hung, L., and Narhi, L. O. (1992). Stability of fungal alpha-amylase in sodium dodecylsulfate. J. Prot. Chem. 11, 111-117.

Arakawa, T., Hung, L., McGinley, M. G., Rohde, M. F., and Narhi, L. O. (1992). Induced resistance of trypsin to sodium dodecylsulfate upon complex formation with trypsin inhibitor. J. Prot. Chem. 11, 171-176.

Arakawa, T., Langley, K. E., Kameyama, K., and Takagi, T. (1992). Molecular weights of glycosylated and nonglycosylated forms of recombinant human stem cell factor determined by low- angle laser light scattering. Anal. Biochem. 203, 53-57.

Carpenter, J. F., Arakawa, T., and Crowe, J. H. (1992). Interactions of stabilizing additives with proteins during freeze- thawing and freeze-drying. Dev.Biol.Stand. 74, 225-238.

Dukor, R. K., Pancoska, P., Keiderling, T. A., Prestrelski, S. J., and Arakawa, T. (1992). Vibrational circular dichroism studies of epidermal growth factor and basic fibroblast growth factor. Arch. Biochem. Biophys. 298, 678-681.

Fox, G. M. and Arakawa, T. (1992). Basic research of fibroblast growth factors. Biomedica 7, 472-477.

Narhi, L. O., Arakawa, T., McGinley, M. D., Rohde, M. F., and Westcott, K. R. (1992). Circular dichroism of reduced and oxidized recombinant human epidermal growth factor. International Journal of Peptide and Protein Research 39, 182-187.

Prestrelski, S. J., Arakawa, T., Wu, C.-S. C., O'Neal, K. D., Westcott, K. R., and Narhi, L. O. (1992). Solution structure and dynamics of epidermal growth factor and transforming growth factor a. J. Biol. Chem. 267 , 319-322.

Prestrelski, S. J., Fox, G. M., and Arakawa, T. (1992). Binding of heparin to basic fibroblast growth factor induces a conformational change. Arch. Biochem. Biophys. 293, 314-319.

Arakawa, T. and Timasheff, S. N. (1991). The interactions of proteins with salts, amino acids and sugars at high concentration. Advances in comparative and environmental physiology 19, 226-245.

Arakawa, T., Lazenby, K., Kolvenbach, C., Horan, T. P., and Narhi, L. O. (1991). [Abnormal migration of subtilisin-Streptomyces subtilisin inhibitor complex during sodium dodecylsulfate polyacrylamide gel electrophoresis. Agric.Biol.Chem. 55, 903-910.

Arakawa, T. and Narhi, L. O. (1991). Solvent modulation in hydrophobic interaction chromatography. Biotechnol.Appl.Biochem. 13, 151-172.

Arakawa, T., Kita, Y. A., and Narhi, L. O. (1991). Protein-ligand interaction as a method to study surface properties of proteins. Methods Biochem.Anal. 35, 87-125.

Arakawa, T., Kita, Y., and Carpenter, J. F. (1991). Protein--solvent interactions in pharmaceutical formulations. Pharm. Res. 8, 285-291.

Arakawa, T., Yphantis, D. A., Lary, J. W., Narhi, L. O., Lu, H. S., Prestrelski, S. J., Clogston, C. L., Zsebo, K. M., Mendiaz, E. A., Wypych, J., and Langley, K. E. (1991). Glycosylated and unglycosylated recombinant-derived human stem cell factors are dimeric and have extensive regular secondary structure. J. Biol. Chem. 266, 18942-18948.

Kolvenbach, C. G., Langley, K. E., Strickland, T. W., Kenney, W. C., and Arakawa, T. (1991). Densimetric determination of carbohydrate content in glycoproteins. J.Biochem.Biophys.Methods 23, 295-300.

Narhi, L. O., Stabinsky, Y., Levitt, M., Miller, L., Sachdev, R., Finley, S., Park, S., Kolvenbach, C., Arakawa, T., and Zukowski, M. (1991). Enhanced stability of subtilisin by three point mutations. Biotechnol.Appl.Biochem. 13, 12-24.

Narhi, L. O., Kenney, W. C., and Arakawa, T. (1991). Conformational changes of recombinant human granulocyte-colony stimulating factor induced by pH and guanidine hydrochloride. J. Prot. Chem. 10, 359-367.

Narhi, L. O., Arakawa, T., Aoki, K. H., Elmore, R., Rohde, M. F., Boone, T., and Strickland, T. W. (1991). The effect of carbohydrate on the structure and stability of erythropoietin. J. Biol. Chem. 266, 23022-23026.

Narhi, L. O., Connor, J., Rohde, M. F., McGinley, M. G., and Arakawa, T. (1991). Stoichiometric complexation of Streptomyces subtilisin inhibitor and subtilisin. J. Prot. Chem. 10, 385-389.

Prestrelski, S. J., Arakawa, T., Kenney, W. C., and Byler, D. M. (1991). The secondary structure of two recombinant human growth factors, platelet-derived growth factor and basic fibroblast growth factor, as determined by Fourier-transform infrared spectroscopy. Arch. Biochem. Biophys. 285, 111-115.

Prestrelski, S. J. and Arakawa, T. (1991). The solution structure and conformational dynamics of tumor necrosis factor-alpha and a (Cys69----Asp; Cys101----Arg) analog as examined by IR spectroscopy and hydrogen exchange. Protein Eng 4, 739-743.

Zhu, X., Komiya, H., Chirino, A., Faham, S., Fox, G. M., Arakawa, T., Hsu, B. T., and Rees, D. C. (1991). Three-dimensional structures of acidic and basic fibroblast growth factors. Science  251, 90-93.

Arakawa, T., Carpenter, J. F., and Crowe, J. H. (1990). Basis for toxicity of certain cryoprotectants: a hypothesis. Cryobiology 27, 401-415.

Arakawa, T. and Horan, T. P. (1990). [Thermal denaturation of subtilisin-SSI complex analyzed by SDS-PAGE. Agric.Biol.Chem. 54, 563-565.

Arakawa, T., Hsu, Y. R., Narachi, M. A., Herrera, C., Rohde, M. F., and Hennigan, P. (1990). Reversibility of acid denaturation of recombinant interferon-gamma. Biopolymers 29, 1065-1068.

Arakawa, T., Visger, J. V., McGinley, M., Rohde, M. F., Fox, G. M., and Narhi, L. O. (1990). Alteration in folding efficiency and conformation of recombinant human tumor necrosis factor-alpha by replacing cysteines 69 and 101 with aspartic acid 69 and arginine 101. Protein Eng 3, 721-724.

Arakawa, T., Horan, T. P., McGinley, M., and Rohde, M. F. (1990). Effect of amino-terminal processing by Staphylococcus aureus V-8 protease on activity and structure of recombinant human interferon- gamma. J.Interferon Res. 10, 321-329.

Arakawa, T., Bhat, R., and Timasheff, S. N. (1990). Preferential interactions determine protein solubility in three- component solutions: the MgCl2 system. Biochemistry 29, 1914-1923.

Arakawa, T., Bhat, R., and Timasheff, S. N. (1990). Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry 29, 1924-1931.

Carpenter, J. F., Crowe, J. H., and Arakawa, T. (1990). Comparison of solute-induced protein stabilization in aqueouis solution and in the frozen and dried states. J.Dairy Sci. 73, 3627-3636.

Elliott, S., Fagin, K. D., Narhi, L. O., Miller, J. A., Jones, M., Koski, R., Peters, M., Hsieh, P., Sachdev, R., Rosenfeld, R. D., Arakawa, T., and Rohde, M. (1990). Yeast-derived recombinant human insulin-like growth factor I: production, purification, and structural characterization. J. Prot. Chem. 9, 95-104.

Kita, Y., Rohde, M. F., Arakawa, T., Fagin, K. D., Fish, E. N., and Banerjee, K. (1990). Characterization of a polyethylene glycol conjugate of recombinant human interferon-gamma. Drug Des Deliv. 6, 157-167.

Kolvenbach, C. G., Narhi, L. O., Lazenby, K., Samal, B., and Arakawa, T. (1990). Comparative study on proteinase R, T, and K from Tritirachiam album limber. International Journal of Peptide and Protein Research 36, 387-391.

Samal, B., Stearns, G., Crandall, C., Arakawa, T., and Boone, T. (1990). Identification of interleukin 6 as a synergistic factor for the differentiation-inducing effect of TNF on leukemic ML-1 cells. Leuk.Res. 14, 575-580.

Arakawa, T., Narachi, M. A., Hsu, Y. R., Everett, R. R., Lai, P. H., and Fish, E. N. (1989). The effect of C-terminal processing on the activity of human interferon- gamma. Drug Des Deliv. 4, 217-225.

Arakawa, T., Hsu, Y. R., Schiffer, S. G., Tsai, L. B., Curless, C., and Fox, G. M. (1989). Characterization of a cysteine-free analog of recombinant human basic fibroblast growth factor. Biochem. Biophys. Res. Commun. 161, 335-341.

Arakawa, T. (1989). The stabilization of beta-lactoglobulin by glycine and NaCl. Biopolymers 28, 1397-1401.

Narhi, L. O. and Arakawa, T. (1989). Sodium dodecyl sulfate polyacrylamide gel electrophoresis as a method for studying the stability of subtilisin. Biochim.Biophys.Acta 990, 144-149.

Narhi, L. O., Kita, Y., and Arakawa, T. (1989). Hydrophobic interaction chromatography in alkaline pH. Anal. Biochem. 182, 266-270.

Narhi, L. O., Rhode, M. F., Hunt, P., and Arakawa, T. (1989). The limited proteolysis of tumor necrosis factor-alpha. J. Prot. Chem. 8, 669-677.

Timasheff, S. N. and Arakawa, T. (1989). Stabilization of protein structure by solvents. In 'Protein structure, a practical approach.' (Ed T. E. Creighton.) pp. 311-345.

Ward, L. D. and Arakawa, T. (1989). Stimulation of microtubule assembly by recombinant human interferon- alpha and interferon-gamma. Biochim.Biophys.Acta 1012, 317-319.

Arakawa, T. and Kenney, W. C. (1988). Secondary structure of interleukin-2(Ala125) in unfolded state. International Journal of Peptide and Protein Research 31, 468-473.

Fish, E. N., Banerjee, K., Arakawa, T., and Stebbing, N. (1988). Structure/function studies on recombinant human gamma interferon. Drug Des Deliv. 2, 191-206.

Fox, G. M., Schiffer, S. G., Rohde, M. F., Tsai, L. B., Banks, A. R., and Arakawa, T. (1988). Production, biological activity, and structure of recombinant basic fibroblast growth factor and an analog with cysteine replaced by serine. J. Biol. Chem. 263, 18452-18458.

Narhi, L. O., Zukowski, M., and Arakawa, T. (1988). Stability of aprA-subtilisin in sodium dodecyl sulfate. Arch. Biochem. Biophys. 261, 161-169.

Timasheff, S. N. and Arakawa, T. (1988). Mechanism of protein precipitation and stabilization by co-solvents. J.Crystal Growth 90, 39-46.

Arakawa, T., Hsu, Y. R., Toth, E., and Stebbing, N. (1987). The antiviral activity of recombinant human tumor necrosis factor-alpha. J.Interferon Res. 7, 103-105.

Arakawa, T. (1987). Effect of cosolvents on solubility of protein in equilibrium between different states. Biopolymers 26, 45-57.

Arakawa, T. and Yphantis, D. A. (1987). Molecular weight of recombinant human tumor necrosis factor-alpha. J. Biol. Chem. 262, 7484-7485.

Arakawa, T., Hsu, Y. R., and Yphantis, D. A. (1987). Acid unfolding and self-association of recombinant Escherichia coli derived human interferon gamma. Biochemistry 26, 5428-5432.

Arakawa, T. and Timasheff, S. N. (1987). Abnormal solubility behavior of beta-lactoglobulin: salting-in by glycine and NaCl. Biochemistry 26, 5147-5153.

Davis, J. M., Narachi, M. A., Alton, N. K., and Arakawa, T. (1987). Structure of human tumor necrosis factor alpha derived from recombinant DNA. Biochemistry 26, 1322-1326.

Davis, J. M., Arakawa, T., Strickland, T. W., and Yphantis, D. A. (1987). Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells. Biochemistry 26, 2633-2638.

Davis, J. M., Narachi, M. A., Levine, H. L., Alton, N. K., and Arakawa, T. (1987). Conformation and stability of two recombinant human interferon-alpha analogs. International Journal of Peptide and Protein Research 29, 685-691.

Narachi, M. A., Davis, J. M., Hsu, Y. R., and Arakawa, T. (1987). Role of single disulfide in recombinant human tumor necrosis factor- alpha. J. Biol. Chem. 262 , 13107-13110.

Narhi, L. O. and Arakawa, T. (1987). Dissociation of recombinant tumor necrosis factor-alpha studied by gel permeation chromatography. Biochem. Biophys. Res. Commun. 147, 740-746.

Yphantis, D. A. and Arakawa, T. (1987). Sedimentation equilibrium measurements of recombinant DNA derived human interferon gamma. Biochemistry 26, 5422-5427.

Arakawa, T., Parker, C. G., and Lai, P. H. (1986). Sites of phosphorylation in recombinant human interferon-gamma. Biochem. Biophys. Res. Commun. 136, 679-684.

Arakawa, T., Hsu, Y. R., Parker, C. G., and Lai, P. H. (1986). Role of polycationic C-terminal portion in the structure and activity of recombinant human interferon-gamma. J. Biol. Chem. 261, 8534-8539.

Arakawa, T. (1986). Thermodynamic analysis of the effect of concentrated salts on protein interaction with hydrophobic and polysaccharide columns. Arch. Biochem. Biophys. 248, 101-105.

Arakawa, T., Boone, T., Davis, J. M., and Kenney, W. C. (1986). Structure of unfolded and refolded recombinant derived [Ala125]interleukin 2. Biochemistry 25, 8274-8277.

Arakawa, T. (1986). Calculation of the partial specific volumes of proteins in concentrated salt, sugar, and amino acid solutions. J. Biochem. (Tokyo) 100, 1471-1475.

Arakawa, T., Hsu, Y. R., Chang, D., Stebbing, N., and Altrock, B. (1986). Structure and activity of glycosylated human interferon-gamma. J.Interferon Res. 6, 687-695.

Hsu, Y. R., Narachi, M., Davis, J. M., Hennigan, P., Goldman, R. A., Geis, A., Carter, M., Stebbing, N., Alton, N. K., and Arakawa, T. (1986). Conformation and biological activity of TNF-alpha and TNF-alpha analogs.  Lymphokine Res. 5 Suppl 1, S133-S137.

Hsu, Y. R., Ferguson, B., Narachi, M., Richards, R. M., Stabinsky, Y., Alton, N. K., Stebbing, N., and Arakawa, T. (1986). Structure and activity of recombinant human interferon-gamma analogs. J.Interferon Res. 6, 663-670.

Lai, P. H., Everett, R., Wang, F. F., Arakawa, T., and Goldwasser, E. (1986). Structural characterization of human erythropoietin. J. Biol. Chem. 261, 3116-3121.

Arakawa, T. and Frieden, C. (1985). The use of the fluorescence photobleaching recovery technique to study the self-assembly of tubulin. Anal. Biochem. 146, 134-142.

Arakawa, T. and Timasheff, S. N. (1985). The stabilization of proteins by osmolytes. Biophysical Journal 47, 411-414.

Arakawa, T. and Goddette, D. (1985). The mechanism of helical transition of proteins by organic solvents. Arch. Biochem. Biophys. 240, 21-32.

Arakawa, T., Alton, N. K., and Hsu, Y. R. (1985). Preparation and characterization of recombinant DNA-derived human interferon-gamma. J. Biol. Chem. 260, 14435-14439.

Arakawa, T. and Timasheff, S. N. (1985). Mechanism of poly(ethylene glycol) interaction with proteins. Biochemistry 24, 6756-6762.

Arakawa, T. and Timasheff, S. N. (1985). Theory of protein solubility. Methods in Enzymology 114, 49-77.

Arakawa, T. (1985). The mechanism of increased elution volume of proteins by polyethylene glycol. Anal. Biochem. 144, 267-268.

Arakawa, T. (1985). [Solvation and properties of proteins]. Tanpakushitsu Kakusan Koso 30, 103-111.

Arakawa, T. and Timasheff, S. N. (1985). Calculation of the partial specific volume of proteins in concentrated salt and amino acid solutions. Methods in Enzymology 117, 60-65.

Hsu, Y. R. and Arakawa, T. (1985). Structural studies on acid unfolding and refolding of recombinant human interferon gamma. Biochemistry 24, 7959-7963.

Arakawa, T. and Timasheff, S. N. (1984). Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding. Biochemistry 23, 5912-5923.

Arakawa, T. and Timasheff, S. N. (1984). Protein stabilization and destabilization by guanidinium salts. Biochemistry 23, 5924-5929.

Arakawa, T. and Frieden, C. (1984). Interaction of microtubule-associated proteins with actin filaments. Studies using the fluorescence-photobleaching recovery technique. J. Biol. Chem. 259, 11730-11734.

Arakawa, T. and Timasheff, S. N. (1984). On protein precipitants. Seibutsubutsuri 24, 29-39.

Arakawa, T. and Timasheff, S. N. (1984). The mechanism of action of Na glutamate, lysine HCl, and piperazine- N,N'-bis(2-ethanesulfonic acid) in the stabilization of tubulin and microtubule formation. J. Biol. Chem. 259, 4979-4986.

Arakawa, T. and Timasheff, S. N. (1983). Preferential interactions of proteins with solvent components in aqueous amino acid solutions.  Arch. Biochem. Biophys. 224, 169-177.

Arakawa, T. and Timasheff, S. N. (1982). Stabilization of protein structure by sugars. Biochemistry 21, 6536-6544.

Arakawa, T. and Timasheff, S. N. (1982). Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 21, 6545-6552.

Arakawa, T. and Timasheff, S. N. (1982). [Mechanism of stabilization of proteins by glycerol and sucrose]. Seikagaku 54, 1255-1259.

Arakawa, T. and Timasheff, S. N. (1982). [On protein-structure stabilizing solvent]. Seikagaku 54, 1307-1310.

Timasheff, S. N., Arakawa, T., Inoue, H., Gekko, K., Gorbunoff, M. J., Lee, J. C., Na, G. C., Pitts, E. P., and Prakashi, V. (1981). The role of solvation in protein structure stabilization and unfolding. Z.Physiol.Chem. 361, 1996.

Arakawa, T., Yoshida, M., Morishita, H., and Yonezawa, D. (1977). [Relation between aggregation behavior of glutenin and its polypeptide composition]. Agric.Biol.Chem. 41, 95-101.

Arakawa, T. (1976). [Comparison of aggregation behavior of glutens from various wheat flours]. New Food Ind. 18, 57-66.

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