Protein Stability in Downstream Processing

Bioseparation and Bioprocessing

Volumn , Issue , 2008, Pages 31-65

  Hejnaes, Kim ^a   Matthiesen, Finn ^a   Skriver, Lars ^a  

^a NONE

Author keywords

Biopharmaceuticals; Downstream; Hydrophobic; Physiological; Reproducibility

Indexed keywords

AFFINITY CHROMATOGRAPHY; ANTIBODIES; BIOACTIVITY; BIOASSAY; CHEMICAL POLISHING; CHEMICAL STABILITY; DEGRADATION; HYDROGEN BONDS; HYDROPHOBICITY; IONIC STRENGTH; LIGANDS; LIPIDS; MATRIX ALGEBRA; NUCLEIC ACIDS; PARAMETER ESTIMATION; PH; REDOX REACTIONS; SODIUM HYDROXIDE; SOLUTIONS; SOLVENTS; SYSTEM STABILITY;

BIOPHARMACEUTICALS; DOWNSTREAM; HYDROPHOBIC; PHYSIOLOGICAL; REPRODUCIBILITIES;

PURIFICATION;

EID: 84955702494     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619641.ch19     Document Type: Chapter

References (159)

1. Pace, C.N., Crit Rev Biochem, 1975, 3, 1-43.
2. Privalov, P.L., Adv Protein Chem, 1979, 33, 167-241.
3. Kauzmann, W., Adv Protein Chem, 1959, 14, 1-63.
4. Pace, C.N., J Mol Biol, 1992, 226, 29-35.
5. Burley, S. K. and Petsko, G. A., Trends Biotechnol, 1989, 7, 354-359.
6. Alber, T., Annu Rev Biochem, 1989, 58, 765-798.
7. Sali, D., Bycroft, M., Ferscht, A.R., J Mol Biol, 1991, 220, 779-788.
8. Serrano, L., Kellis, J.T. Jr., Cann, P., Matouschek, A., Ferscht, A.R., J Mol Biol, 1992, 224, 783-804.
9. Matthews, B.W., Curr Opin Struct Biol, 1993, 3, 589-593.
10. Stickle, D.F., Presta, L.G., Dill, K.A., Rose, G.D., J Mol Biol, 1992, 226, 1143-1159.
11. Shirley, B.A., Stanssens, P., Hahn, U., Pace, C.N., Biochemistry, 1992, 31, 725-732.
12. Dill, K.A., Biochemistry, 1990, 29, 7133-7155.
13. Burley, S.K., Petsko, G.A., Science, 1985, 229, 23-28.
14. Creighton, T.E., Biopolymers, 1983, 22, 49-58.
15. Privalov, P.L., Annu Rev Biophys Chem, 1989, 18, 47-69.
16. Creighton, T.E., Curr Opin Struct Biol, 1991, 1, 5-16.
17. Richards, F.M., Annu Rev Biophys Bioeng, 1977, 6, 151-176.
18. Rose, G.D., Annu Rev Biophys Biomol Struct, 1993, 22, 381-415.
19. Baker, E.N., Hubbard, R.E., Prog Biophys Molec Biol, 1984, 44, 97-179.
20. Chothia, C., J Mol Biol, 1976, 105, 1-14.
21. Matthews, B.W., Nat Struct Biol, 1995, 2, 85-86.
22. Creighton, T.E., J Phys Chem, 1985, 89, 2452-2459.
23. Matthews, B.W., Curr Opin Struct Biol, 1991, 1, 17-21.
24. Jaenicke, R., Eur J Biochem, 1991, 202, 715-728.
25. Seckler, R., Jaenicke, R., FASEB J, 1992, 6, 2545-2552.
26. Oobatake, M., Tatsuo, O., Prog Biophys Mol Biol, 1993, 59, 237-284.
27. Ptitsyn, O.B., Uversky, V.N., FEBS Lett, 1994, 341, 15-18.
28. Privalov, P.L., Adv Protein Chem, 1979, 33, 167-241.
29. Jaenicke, R., Prog Biophys Mol Biol, 1987, 49, 117-237.
30. Creighton, T.E., Biochem J, 1990, 270, 1-16.
31. Shortle, D., FASEB J, 1996, 10, 27-34.
32. Neri, D., Billeter, M., Wider, G., Wüthrich, K., Science, 1992, 257, 1559-1563.
33. Creighton, T. E., in: Mechnisms of Protein Folding: Pain, R.H. (Ed.), Oxford: IRL Press, 1994; pp. 1-25.
34. Brange, J., Andersen, K., Laursen, E. D., Meyn, G., Rasmussen, E., J. Pharm Sci, 1997, in press.
35. North, M. J., in: Proteolytic Enzymes - a practical approach: Beynon, R.J., Bond, J.S. (Eds.), Oxford: IRL Press, 1989; pp. 105-124.
36. Battersby, J.E., Hancock, W. S., Canova-Davis, E., Oeswein, J., O'Connor, B., Int Peptide Protein Res, 1994, 44, 215-222.
37. Schultz, J., Methods Enzymol, 1967, 11, 255-263.
38. Piszkiewicz, D., Landon, M., Smith, E. L., Biochem Biophys Res Commun, 1970, 40, 1173- 1178.
39. Whitaker, J.R., Feeney, R.E., Crit Rev Food Sci Nutr, 1983, 19, 173-212.
40. Hayashi, R., Kameda, I., Agric Biol Chem, 1980, 44, 175-181.
41. Berson, S.A., Yalow, R.S., Diabetes, 1966, 15, 875-879.
42. Brange, J., Langkjaer, L., Havelund, S., Voelund, A., Pharm Res, 1992, 9, 715-726.
43. Lewis, U. J., Cheever, E.V., Hopkins, W.C., Biochim Biophys Acta, 1970, 214, 498-508.
44. Flatmark, T., Acta Chem Scand, 1966, 20, 1487-1496.
45. Geiger, T., Clarke, S., J Biol Chem, 1987, 262, 785-794.
46. Clarke, S., Stephenson, R. C., Lowenson, J. D., in: Stability of Protein Pharmaceuticals: Ahern, T. J., Manning, M.C., (Eds.), New York: Plenum Press, 1992; Part A, pp. 1-29.
47. Chazin, W. J., Kossiakoff, A.A., in: Deamidation and Isoaspartate Formation in Peptides and Proteins: Aswad, D.W. (Ed.), London: CRC Press, 1995; pp. 194-206.
48. Slobin, L.I., Carpenter, F.H., Biochemistry, 1963, 2, 22-28.
49. Brennan, T. V., Clarke, S., in: Deamidation and Isoaspartate Formation in Peptides and Proteins: Aswad, D.W. (Ed.), London: CRC Press, 1995, pp. 66-90.
50. Yüksel, K.U., Gracy, R.W., Arch Biochem Biophys, 1986, 248, 452-459.
51. Bhatt, N.P., Patel, K., Borchardt, R.T., Pharm Res, 1990, 7, 593-599.
52. Robinson, A.B., Rudd, C. J., in: Current Topics in Cellular Regulation: Horecker, B.L. and Stadtmann, E.R., (Eds.), New York: Academic Press, 1974; pp. 247-295.
53. Manning, M.C., Patel, K., Borchardt, R.T., Pharm Res, 1989, 6, 903-918.
54. Wright, H.T., Protein Eng, 1991, 4, 283-294.
55. Johnson, B. A., Aswad, D. W., in: Deamidation and Isoaspartate Formation in Peptides and Proteins: Aswad, D.W. (Ed.), London: CRC Press, 1995; pp. 91-113.
56. Becker, G. W., Tackitt, P. M., Bromer, W. W, Lefeber, D. S., Riggin, R. M., Biotech Appl Biochem, 1988, 10, 326-337.
57. Scotchler, J.W., Robinson, A.B., Anal Biochem, 1974, 59, 319-322.
58. Sen, L. C, Gonzalez-Flores, E., Feeney, R. E., Whitaker, J. R., J Agric Food Chem, 1977, 25,632-638.
59. Lee, H.S., Osuga, D.T., Nashef, A.S., Ahmed, A. I., Whitaker, J.R., Feeney, R.E., J Agric Food Chem, 1977, 25, 1153-1158.
60. Nashef, A. S., Osuga, D.T., Lee, H.S., Ahmed, A. I., Whitaker, J.R., Feeney, R.E., J Agric Food Chem, 1977, 25, 245-251.
61. Volkin, D.B., Klibanov, K.M., J Biol Chem, 1987, 262, 2945-2950.
62. Masters, P.M., Friedman, M., ACS Symp Ser, 1980, 123, 165-194.
63. Hayashi, R., Kameda, I., Agric Biol Chem, 1980, 44, 891-895.
64. Dedman, M.L., Farmer, T.H., Morris, C.J.O.R., Biochem J, 1961, 78, 348-352.
65. Tashijan, A.H.J., Ontjes, D. A., Munson, P.L., Biochemistry, 1964, 3, 1175-1182.
66. Morley, J.S., Tracy, H.J., Gregory, R.A., Nature, 1965, 207, 1356-1359.
67. Brot, N., Weissbach, H., Trends Biochem Sci, 1982, 7, 137-139.
68. Cleland, J.L., Powell, M.F., Shire, S. J., Crit Rev Ther Drug Carrier Sys, 1993, 10, 307- 377.
69. Gilbert, H.F., Adv Enzymol, 1990, 63, 69-172.
70. Wold, F., Macromolecules: Structure and Function. London: Prentice-Hall, Inc. 1971; pp. 53-89.
71. Martin, B.M., Viswanatha, T., Biochem Biophys Res Commun, 1975, 63, 247-253.
72. Torchinsky, Y. M., in: Sulfur in Proteins: Metzler, D. (Ed.), Oxford: Pergamon Press, 1995; pp. 199-217.
73. Shaked, Z., Szajewski, R.P., Whitesides, G.M., Biochemistry, 1980, 19, 4156-4166.
74. Soerensen, H. H., Thomsen, J., Bayne, S., Hoejrup, P., Roepstorff, P., Biomed Environ Mass Spec, 1990, 19, 713-720.
75. Benesch, R.E., Benesch, R., J Am Chem Soc, 1958, 80, 1666-1669.
76. Florence, T. M., Biochem J, 1980, 189, 507-520.
77. Torchinsky, Y. M., in: Sulfurin Proteins: Metzler, D. (Ed.), Oxford: Pergamon Press, 1981; pp. 57-65.
78. Misra, H. P., J Biol Chem, 1974, 249, 2151-2155.
79. Jespersen, A.M., Christensen, T., Klausen, N.K., Nielsen, P.F., Soerensen, H.H., Eur J Biochem, 1994, 219, 365-373.
80. Tanford, C., Adv Protein Chem, 1968, 23, 218-281.
81. O'Fágáin, C., Sheehan, H., O'Kennedy, R., Kilty, C., Process Biochem, 1988, XX, 166-171.
82. Kunth, I.D.J., in: The Protein Folding Problem: Wetlaufer, D.B. (Ed.), AAAS Selected Symposium 89, 1984; pp. 65-81.
83. Matthiesen, F., Hejnaes, K.R., Skriver, L., Ann N Y Acad Sci, 1996, 782, 413-421.
84. Hejnaes, K.R., Bayne, S., Noerskov, L., et al., Protein Eng, 1992, 5, 797-806.
85. Kiefhaber, T., Rudolph, R., Kohier, H.-H., Buchner, J., Biotechnology, 1991, 9, 825-829.
86. Jaenicke, R., in: Protein Conformation: New York: John Wiley and Sons, 1991, pp. 206-217.
87. Oliveberg, M., Fersht, A.R., Biochemistry, 1996, 35, 2738-2749.
88. Speed, M. A., Wang, D.I.C., King, J., Nat Biotech, 1996, 14, 1283-1287.
89. De Young, L.R., Dill, K.A., Fink, A.L., Biochemistry, 1993, 32, 3877-3886.
90. Moody, A. J., Hejnaes, K.R., Marshall, M. O. et al, Diabetologia, 1995, 38, 14-23.
91. Chou, P. Y., Fasman, G.D., Biochemistry, 1975, 14, 2536-2541.
92. Zettlmeissl, G., Rudolph, R., Jaenicke, R., Biochemistry, 1979, 18, 5567-5571.
93. DeFelippis, M.R., Alter, L.A., Pekar, A.H., Havel, H.A., Brems, D.N., Biochemistry, 1993, 32, 1555-1562.
94. Sluzky, V., Klibanov, A.M., Langer, R., Biotech and Bioeng, 1992, 40, 895-903.
95. Mendoza, J.A., Rogers, E., Lorimer, G.H., Horowitz, P.M., J Biol Chem, 1991, 266, 13587-13591.
96. Bai, Y, Milne, J. S., Mayne, L., Englander, S.W., Proteins, 1994, 20, 4-14.
97. Cleland, J.L., Wang, I.C., Biochemistry, 1990, 29, 11072-11078.
98. Tandon, S., Horowitz, P., J Biol Chem, 1986, 261, 15615-15681.
99. Hartley, D.L., Kane, J.F., Biochem Soc Trans, 1988, 16, 101-102.
100. Scopes, R. K., in: Protein Purification - Principles and Practice: New York: Springer-Verlag, 1987; pp. 41-71.
101. Hoffmeister, F., Naun-Schmiedelberg's Archiv Pharmak. Exp. Patholog (Leipzig), 1988, 24, 249-260.
102. Pace, C.N., Trends Biochem Sci, 1990, 15, 14-17.
103. Becktel, W. J., Schellman, J. A., Biopolymers, 1987, 26, 1859-1877.
104. Doty, P., Imahori, K., Klemperer, E., Proc Natl Acad Sci USA, 1958, 44, 424-431.
105. Hippel, P. H., Schleich, T., in: Structure and Stability of Biological Macromolecules: Timasheff, S.N., Fasman, G.D. (Eds.). New York: Marcel Dekker Inc. 1969; pp. 417-557.
106. Tombs, M. P., J Appl Biochem, 1985, 7, 3-24.
107. Sundby, R., J Biol Chem, 1962, 237, 3406-3411.
108. Wheelock, E.F., Science, 1965, 149, 310-311.
109. Hoshino, T., Mikura, Y., Shimidzu, H., Kusumoto, S., Kawai, J., Toguchi, H., Biochim Biophys Acta, 1987, 916, 245-250.
110. Shami, E. Y., Rothstein, A., Ramjeesingh, M., Trends Biotechnol, 1989, 7, 186-190.
111. Whitaker, J.R., ACS Symp Ser, 1980, 123, 145-163.
112. Chalikian, T.V., Gindikin, V.S., Breslauer, K.J., FASEB J, 1996, 10, 164-170.
113. Porter, W.R., Staack, H., Brand, K., Manning, M.C., Thromb Res, 1993, 71, 265-279.
114. Janin, J., Colloids and Surfaces, 1984, 10, 1-7.
115. Makhatadze, G.I., Privalov, P.L., J Mol Biol, 1993, 232, 639-659.
116. Shellmann, J. A., Lindorfer, M., Hawkes, R., Grutter, M., Biopolymers, 1981, 20, 1989-1999.
117. Privalov, P.L., Khechinashvili, N.N., J Mol Biol, 1974, 86, 665-684.
118. Privalov, P.L., Griko, Y.V., Venyaminov, S.Y., Kutyshenko, V.P., J Mol Biol, 1986, 190, 487-498.
119. Hermans, J. J., Scheraga, H.A., J Am Chem Soc, 1961, 83, 3283-3292.
120. Volkin, D. B., Middaugh, C.R., in: Stability of Protein Pharmaceuticals:
121. Baldwin, R.L., Eisenberg, D., in: Protein Engineering: Oxender, D. L., Fox, C.F. (Eds.), New York: Alan R. Liss, Inc, 1987; pp. 127-148.
122. Tomazic, S.J., Klibanov, A.M., J Biol Chem, 1988, 263, 3086-3091.
123. Zale, S.E., Klibanov, A.M., Biochemistry, 1986, 25, 5432-5444.
124. Cleland, W.W., Biochemistry, 1964, 3, 480-482.
125. Scott, E.M., Duncan, I.W., Ekstrand, V., J Biol Chem, 1963, 238, 3928-3933.
126. th ed. New York: 1996; pp. 8.21-8.33.
127. Dutton, P.L., Methods Enzymol, 1978, 54, 411-435.
128. Maeda, Y., Yamada, H., Ueda, T., Imoto, T., Protein Eng, 1996, 9, 461-465.
129. Hospelhorn, V.D., Cross, B., Jensen, E.V., J Am Chem Soc, 19854, 76, 2827-2829.
130. Timasheff, S.N., in: Stability of Protein Pharmaceuticals: Ahern, T. J., Manning, M.C. (Eds.), New York: Plenum Press, 1992; Part B, pp. 265-285.
131. Arakawa, T., Prestrelski, S. J., Kenney, W. C., Carpenter, J. F., Adv Drug Del Rev, 1993, 10, 1-28.
132. Arakawa, T.R., Timasheff, S.N., Biochemistry, 1985, 24, 6756-6762.
133. Pittz, E.P., Timasheff, S.N., Biochemistry, 1978, 17, 615-623.
134. London, J., Skrzynia, C., Goldberg, M.E., Eur J Biochem, 1974, 47, 409-415.
135. Brems, D.N., Havel, H.A., Proteins, 1990, 5, 93-95.
136. Buchner, J., Rudolph, R., Biotechnology, 1991, 9, 157-162.
137. Winkler, M.E., Blaber, M., Biochemistry, 1986, 25, 4041-4045.
138. Zardeneta, G., Horowitz, P.M., J Biol Chem, 1992, 267, 5811-5816.
139. Kristjansson, M.M., Kinsella, J. E., Adv Food Nutr Res, 1991, 35, 237-316.
140. Timasheff, S.N., Annu Rev Biomol Struct, 1993, 22, 67-97.
141. Lougheed, W.D., Albisser, A.M., Martindale, H.M., Chow, J.C., Clement, J.R., Diabetes, 1983, 32, 424-432.
142. Tandon, S., Horowitz, P.M., J Biol Chem, 1989, 264, 9859-9866.
143. Tandon, S., Horowitz, P.M., J Biol Chem, 1987, 262, 4486-4491.
144. Jirgensons, B., J Biol Chem, 1967, 242, 912-918.
145. Hunt, A.H., Jirgensons, B., Biochemistry, 1973, 12, 4435-4441.
146. Jirgensons, B., J Protein Chem, 1982, 1, 71-84.
147. Ryabova, L. A., Desplancq, D., Spirin, A. S., Plückthun, A., Biochemistry, 1997, 15, 79-84.
148. Timasheff, S.N., Annu Rev Biophys Biomol Struct, 1993, 22, 67-97.
149. Arakawa, T., Bhat, R., Timasheff, S.N., Biochemistry, 1990, 29, 1914-1923.
150. Timasheff, S.N., in: Protein-Solvent Interactions. Gregory, R. B. (Ed.), New York: Marcel Dekker, Inc., 1994; pp. 445-482.
151. Beaven, G. H., Gratzer, W.B., Davies, H. G., Eur J Biochem, 1969, 121, 37-42.
152. Heremans, K., Annu Rev Biophys Bioeng, 1982, 11, 1-21.
153. Silva, J.L., Annu Rev Phys Chem, 1993, 44, 90-113.
154. Gross, M., Jaenicke, R., Eur J Biochem, 1994, 221, 617-630.
155. Goossens, K., Smeller, L., Frank, J., Heremans, K., Eur J Biochem, 1996, 236, 254-262.
156. Takeda, N., Kato, M., Taniguchi, Y., Biochemistry, 1995, 34, 5980-5987.
157. Montgomery, D. C., in: Design and Analysis of Experiments: New York: John Wiley Sons, 1991; pp. 197-249.
158. Clonis, Y.D., Stead, C.V., Lowe, C.R., Biotech Bioeng, 1987, 30, 621-627.
159. Lowe, C. R., Burton, S. J., Burton, N. P., Alderton, W. K., Pitts, J. M., Thomas, J. A., Trends Biotechnol, 1992, 10, 442-448.