Arakawa T - Search Results

1

Solvent modulation of column chromatography.

Arakawa T, Kita Y, Ejima D, Gagnon P. Arakawa T, et al. Protein Pept Lett. 2008;15(6):544-55. doi: 10.2174/092986608784966994. Protein Pept Lett. 2008. PMID: 18680448 Review.

2

Characterization of a polyethylene glycol conjugate of recombinant human interferon-gamma.

Kita Y, Rohde MF, Arakawa T, Fagin KD, Fish EN, Banerjee K. Kita Y, et al. Among authors: arakawa t. Drug Des Deliv. 1990 Sep;6(3):157-67. Drug Des Deliv. 1990. PMID: 1963781

3

Protein-ligand interaction as a method to study surface properties of proteins.

Arakawa T, Kita YA, Narhi LO. Arakawa T, et al. Methods Biochem Anal. 1991;35:87-125. doi: 10.1002/9780470110560.ch2. Methods Biochem Anal. 1991. PMID: 2002772 Review. No abstract available.

4

Solvent modulation in hydrophobic interaction chromatography.

Arakawa T, Narhi LO. Arakawa T, et al. Biotechnol Appl Biochem. 1991 Apr;13(2):151-72. Biotechnol Appl Biochem. 1991. PMID: 2043277 Review.

5

Protein--solvent interactions in pharmaceutical formulations.

Arakawa T, Kita Y, Carpenter JF. Arakawa T, et al. Pharm Res. 1991 Mar;8(3):285-91. doi: 10.1023/a:1015825027737. Pharm Res. 1991. PMID: 2052513 Review.

6

Hydrophobic interaction chromatography in alkaline pH.

Narhi LO, Kita Y, Arakawa T. Narhi LO, et al. Among authors: arakawa t. Anal Biochem. 1989 Nov 1;182(2):266-70. doi: 10.1016/0003-2697(89)90592-7. Anal Biochem. 1989. PMID: 2610344

7

Contribution of the surface free energy perturbation to protein-solvent interactions.

Kita Y, Arakawa T, Lin TY, Timasheff SN. Kita Y, et al. Among authors: arakawa t. Biochemistry. 1994 Dec 20;33(50):15178-89. doi: 10.1021/bi00254a029. Biochemistry. 1994. PMID: 7999778

The high values of preferential hydration found in all cases, except for BSA in ArgHCl, suggest that they should stabilize protein structure, as had been found for lysine hydrochloride and monosodium glutamate [Arakawa, T., & Timasheff, S. N. (1984) J. Biol. Che …

The high values of preferential hydration found in all cases, except for BSA in ArgHCl, suggest that they should stabilize protein structure …

8

Conformation of glutathione adduct and oxidized forms of platelet-derived growth factor.

Narhi LO, Kenney WC, Prestrelski SJ, Arakawa T, Lyons D, Lary J, Yphantis DA. Narhi LO, et al. Among authors: arakawa t. Int J Pept Protein Res. 1993 Jan;41(1):8-14. doi: 10.1111/j.1399-3011.1993.tb00109.x. Int J Pept Protein Res. 1993. PMID: 8436449

9

ErbB receptor activation, cell morphology changes, and apoptosis induced by anti-Her2 monoclonal antibodies.

Kita Y, Tseng J, Horan T, Wen J, Philo J, Chang D, Ratzkin B, Pacifici R, Brankow D, Hu S, Luo Y, Wen D, Arakawa T, Nicolson M. Kita Y, et al. Among authors: arakawa t. Biochem Biophys Res Commun. 1996 Sep 4;226(1):59-69. doi: 10.1006/bbrc.1996.1311. Biochem Biophys Res Commun. 1996. PMID: 8806592

10

Effect of three elution buffers on the recovery and structure of monoclonal antibodies.

Narhi LO, Caughey DJ, Horan T, Kita Y, Chang D, Arakawa T. Narhi LO, et al. Among authors: arakawa t. Anal Biochem. 1997 Nov 15;253(2):236-45. doi: 10.1006/abio.1997.2375. Anal Biochem. 1997. PMID: 9367509

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