Conformational Properties of Disulfide-Free Recombinant Chicken Ovalbumin

Journal of Biochemistry and Molecular Biology

Volumn 32, Issue 3, 1999, Pages 247-253

  Jeoung, Yeon Hee ^a   Yu, Myeong Hee ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

Conformational stability; High level expression; Ovalbumin

Indexed keywords

EID: 0033420201     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (40)

1. Abraham, C. R., Selkoe, D. J. and Potter, H. (1988) Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 52, 487-501.
2. Ahmad, F. and Salahuddin, A. (1976) Reversible unfolding of the major fraction of ovalbumin by guanidine hydrochloride. Biochemistry 15, 5168-5175.
3. 1-antichymotrypsin at 2.7 Å resolution and its comparison with other serpins. J. Mol. Biol. 218, 595-606.
4. Bruch, M., Weiss, V. and Engel, J. (1988) Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites. J. Biol. Chem. 263, 16626-16630.
5. 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis. Nature 317, 730-732.
6. Carrell, R. W., Stein, P. E., Fermi, G. and Wardell, M. R. (1994) Biological implications of a 3 Å structure of dimeric antithrombin. Structure 2, 257-270.
7. Chang, J. Y. (1997) A two-stage mechanism for the reductive unfolding of disulfide-containing proteins. J. Biol. Chem. 272, 69-75.
8. 1,-Antichymotrypsin regulates Alzheimer β-amyloid peptide fibril formation. Proc. Natl. Acad. Sci. USA 92, 2313-2317.
9. Gettins, P. (1989) Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin. J. Biol. Chem. 264, 3781-3785.
10. Goldenberg, D. P. (1989) Analysis of protein conformation by gel electrophoresis. In Protein Structure: A Practical Approach. Creighton, T. E. (ed.), pp. 225-250, IRL Press, New York.
11. Heimark, R. L., Kurachi, K., Fujikawa, K. and Davie, E. W. (1980) Nature 286, 456-460.
12. 1-antitrypsin for structure and function of serpins. Biochemistry 28, 8951-8966.
13. 1-antitrypsin cDNA in yeast Saccharomyces cerevisiae. Korean Biochem. J. (presently J. Biochem. Mol. Biol.) 23, 263-268.
14. 1-antitrypsin suppresses the folding defect of the Z-type variant. J. Biol. Chem. 270, 8597-8601.
15. Klausner, R. D., Kempf, C., Weinsrein, J. N., Blumenthal, R. and Van Renswoude, J. (1983) The folding of ovalbumin. Renaturation in vitro versus biosynthesis in vitro. Biochem. J. 212, 801-810.
16. Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492.
17. 1-antitrypsin that confer enhancement in thermal stability. J. Biol. Chem. 269, 9627-9631.
18. 1-antitrypsin. Ph.D. thesis. Seoul National University, Seoul, Korea.
19. Lee, K. N., Park, S. D. and Yu, M. H. (1996) Probing the native strain in alpha 1-antitrypsin. Nat. Struct. Biol. 3, 497-500.
20. 1-antitrypsin cDNA and its expression in Escherichia coli. Korean Biochem. J. (presently J. Biochem. Mol. Biol.) 22, 148-153.
21. 1-proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177, 531-556.
22. Ma, L., Yee, A., Brewer, H. B. Jr., Das, S. and Potter, H. (1994) Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372, 92-94.
23. Munch, M., Heegaard, C., Jensen, P. H. and Andreasen, P. A. (1991) Type-1 inhibitor of plasminogen activators. Distinction between latent, activated and reactive center-cleaved forms with thermal stability and monoclonal antibodies. FEBS Lett. 295, 102-106.
24. Onda, M., Tatsumi, E., Takahashi, N. and Hirose, M. (1997) Refolding process of ovalbumin from urea-denatured state. Evidence for the involvement of nonproductive side chain interactions in an early intermediate. J. Biol. Chem. 272, 3973-3979.
25. Pemberton, P. A., Stein, P. E., Pepys, M. B., Potter, J. M. and Carrell, R. W. (1988) Hormone binding globulins undergo serpin conformational change in inflammation. Nature 336, 257-258.
26. Pemberton, P. A., Wong, D. T., Gibson, H. L., Kiefer, M. C., Fitzpatrick, P. A., Sager, R. and Barr, P. J. (1995) The tumor suppressor Maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. J. Biol. Chem. 270, 15832-15837.
27. Schreuder, H. A., de Boer, B., Dijkema, R., Mulders, J., Theunissen, H. J., Grootenhuis, P. D. and Hol, W. G. (1994) The intact and cleaved human antithrombin III complex as a model for serpin-protease interactions. Nat. Struct. Biol. 1, 48-54.
28. 1-antitrypsin reveals the conformation of its inhibitory reactive loop. FEBS Lett. 377, 150-154.
29. Stefansson, S. and Lawrence, D. A. (1996) The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin. Nature 383, 441-443.
30. Stein, P. E. and Carrell, R. W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease? Nat. Struct. Biol. 2, 96-113.
31. Stein, P. E., Leslie, A. G., Finch, J. T., Turnell, W. G., McLaughlin, P. J. and Carrell, R. W. (1990) Crystal structure of ovalbumin as a model for the reactive center of serpins. Nature 347, 99-102.
32. Takahashi, N. and Hirose, M. (1992) Reversible denaturation of disulfide-reduced ovalbumin and its reoxidation generating the native cystine cross-link. J. Biol. Chem. 267, 11565-11572.
33. Takahashi, N., Orita, T. and Hirose, M. (1995) Production of chicken ovalbumin in Escherichia coli. Gene 161, 211-216.
34. Vaux, D. L., Haecker, G. and Strasser, A. (1994) An evolutionary perspective on apoptosis. Cell 76, 777-779.
35. Wei, A., Rubin, H., Cooperman, B. S. and Christianson, D. W. (1994) Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nat. Struct. Biol. 1, 251-258.
36. Wright, H. T. (1984) Ovalbumin is an elastase substrate. J. Biol. Chem. 259, 14335-14336.
37. Wright, H. T., Quian, H. X. and Huber, R. (1990) Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved alpha-1-proteinase inhibitor. J. Mol. Biol. 213, 513-528.
38. Wright, H. T. and Scarsdale, J. N. (1995) Structural basis for serpin inhibitor activity. Proteins 22, 210-225.
39. 1-antitrypsin causes a protein folding defect. Nat. Struct. Biol. 2, 363-367.
40. Zou, Z., Anisowicz, A., Hendrix, M. J. C., Thor, A., Neveu, M., Sheng, S., Rafidi, K., Seftor, E. and Sager, R. (1994) Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. Science 263, 526-529.