REFERENCES
J. F. Carpenter, J. H. Crowe, and T. Arakawa. Comparison of solute-induced protein stabilization in aqueous-solution and in the frozen and dried states. J. Dairy Sci. 73:3627–3636 (1990).
J. H. Crowe, J. F. Carpenter, L. M. Crowe, and T. J. Anchordoguy. Are freezing and dehydration similar stress vectors? A comparison of modes of interaction of stabilizing solutes with biomolecules. Cryobiology. 27:219–231 (1990).
M. Z. Zhang, J. Wen, T. Arakawa and S. J. Prestrelski. 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 (1995).
M. W. Townsend and P. P. DeLuca. Stability of ribonuclease A in solution and the freeze-dried state. J. Pharm. Science. 79:1083–1086 (1990).
M. A. Kunitz. A spectrophotometric method for the measurement of ribonuclease activity. J. Biol. Chem. 164:563–568 (1946).
A. Wang, S. Lu, and D. F. Mark. Site-specific mutagenesis of the human interleukin-2 gene: Structure-function analysis of the cysteine residues. Science. (Washington, D.C) 224:1431–1433 (1984).
S. Hora, P. K. Rana, Cynthia L. Wilcox, N. V. Katre, Pamela Hirtzer, S. N. Wolfe and J. W. Thomson. Development of a lyophilized formulation of interleukin-2. Develop. Biol. Standard. 74:295–306 (1991).
S. J. Prestrelski, K. A. Pikal and T. Arakawa. Optimization of lyophilization conditions for interleukin-2. Submitted for publication.
R. E. Dickerson, I. Geis. The structure and action of proteins. Harper and Row: New York, 79 (1969).
G. Kartha, J. Bello, and D. Harker. Tertiary structure of ribonuclease. Nature 213:862–865 (1967).
M. C. Lin. The structural role of amino acid residues near the carboxyl terminus of bovine pancreatic ribonuclease A. J. Biol. Chem., 245:6726–6731 (1970).
M. S. Wang, R. D. Gandour, J. Rodgers, J. L. Haslam, and R. L. Schowen. Transition-state structure for a conformation change of ribonuclease. Bioorg. Chem. 4:392–406 (1975).
M. W. Townsend, P. R. Byron, P. P. DeLuca. Nature of aggregates formed during storage of freeze-dried ribonuclease A. J. Pharm. Science. 7:63–66 (1991).
M. W. Townsend, P. R. Byron, P. P. DeLuca. Stability of ribonuclease A in solution and the freeze-dried state. J. Pharm. Science. 7:1083–1086 (1990).
A. M. Crestfield, W. H. Stein, S. Moore. On the aggregation of bovine pancreatic ribonuclease. Arch. Biochem. Biophys. suppl. 1:217–222 (1962).
B. A. Alberty, E. A. Anderson, and J. W. Williams. Homogeneity and the electrophorectic behavior of some protein. J. Phys. and Colloid Chem. 52:217–230 (1948).
A. M. Crestfield, and F. W. Allen. Studies of the mobility of ribonclease by zone electrophoresis. J. Biol. Chem. 211:363–366 (1954).
M. A. Rosemayer and E. M. Shooter. An electrophoretic investigation of ribonuclease. Biochem. J. 69:28p–29p (1958).
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Zhang, M.Z., Pikal, K., Nguyen, T. et al. The Effect of the Reconstitution Medium on Aggregation of Lyophilized Recombinant Interleukin-2 and Ribonuclease A. Pharm Res 13, 643–646 (1996). https://doi.org/10.1023/A:1016074811306
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DOI: https://doi.org/10.1023/A:1016074811306