Conformational state of disulfide-reduced ovalbumin at acidic pH

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 7, 1999, Pages 1285-1290

  Tatsumi, Eizo ^a,b   Yoshimatsu, Daisuke ^a   Hirose, Masaaki ^a  

^a KYOTO UNIVERSITY   (Japan)

^b JAPAN INTERNATIONAL RESEARCH CENTER FOR AGRICULTURAL SCIENCES   (Japan)

Author keywords

Conformational stability; Conformational state; Disulfide reduction; Molten globule; Ovalbumin

Indexed keywords

DISULFIDE; OVALBUMIN; PEPSIN A; TRYPTOPHAN;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE; GEL CHROMATOGRAPHY; HYDROLYSIS; OXIDATION REDUCTION REACTION; PH; PROTEIN CONFORMATION;

CALORIMETRY, DIFFERENTIAL SCANNING; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; DISULFIDES; FLUORESCENCE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; OVALBUMIN; OXIDATION-REDUCTION; PEPSIN A; PROTEIN CONFORMATION; TRYPTOPHAN;

EID: 0033160339     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1285     Document Type: Article

References (32)

1. Tanford, C., Protein dénaturation. In “Advances in Protein Chemistry”, eds. Anfinsen, C. B., Jr., Edsall, J. T., and Richards, F. M., Academic Press, New York, Vol. 24, pp. 1-95 (1970).
2. Kuwajima, K., The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Fund. Genet., 6, 87-103 (1989).
3. Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, E., and Razgulyaev, O. I., Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett., 262, 20-24 (1990).
4. Dolgikh, D. A., Gilmanshin, R. I., Brazhnikov, V. E., Bychkova, G. V., Semisotnov, G. V., Venyaminov, S. Yu, and Ptitsyn, O. B., α-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Lett., 136, 311-315 (1981).
5. Ohgushi, M. and Wada, A., ‘Molten-globule state’: a compact form of globular proteins with mobile side-chains. FEBS Lett., 164, 21-24 (1983).
6. Hirose, M., Molten globule state of food proteins. Trends Food Sci. Techno!., 4, 48-51 (1993).
7. Yutani, K., Ogasahara, K., and Kuwajima, K., Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. J. Mol. Biol., 228, 347-350 (1992).
8. Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F., and Goto, Y., Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol., 249, 215-228 (1995).
9. Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas’, A. F., and Gilmanshin, R. I., Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers, 31,119-128 (1991).
10. Van Dael, H., Haezebrouck, P., Morozova, L., Arico-Muendel, C., and Dobson, C. M., Partially folded states of equine lysozyme. Structural characterization and significance for protein folding. Biochemistry, 32, 11886-11894 (1993).
11. Griko, Y. V., Freire, E., Privalov, G., Van Dael, H., and Privalov, P. L., The unfolding thermodynamics of otype lysozyme: a calorimetric study of the heat dénaturation of equine lysozyme. J. Mol. Biol., 252, 447-459 (1995).
12. Hamada, D., Kidokoro, S., Fukada, H., Takahashi, K., and Goto, Y., Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl. Acad. Sci. USA, 91, 10325-10329 (1994).
13. Uversky, V. N. and Ptitsyn, O. B., “Partly folded” state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of /Mactamase at low temperature. Biochemistry, 33, 2782-2791 (1994).
14. Uversky, V. N. and Ptitsyn, O. B., Further evidence on the equilibrium “pre-molten globule state”: four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. J. Mol. Biol., 255, 215-218 (1996).
15. Jeng, M.-F. and Englander, S. W., Stable submolecular folding units in a non-compact form of cytochrome c. J. Mol. Biol., 221, 1045-1061 (1991).
16. R. O’Donnell, The ovalbumin family of serpin proteins. FEBS Lett., 315, 105-108 (1993).
17. Stein, P. E., Leslie, A. G. W., Finch, J. T„ and Carrell, R. W., Crystal structure of uncleaved ovalbumin at 1.95 A resolution. J. Mol. Biol., 221, 941-959 (1991).
18. Koseki, T., Kitabatake, N., and Doi, E., Conformational changes in ovalbumin at acid pH. J. Biochem., 103, 425-430 (1988).
19. Doi, E., Koseki, T., Tani, F., Kitabatake, N., Nemoto, N., Koike, A., Fukada, H., and Takahashi, K., Molten globule-like conformation of ovalbumin at acidic pHs. In “Abstract for 43rd Tanpakushitsu Kozo Toronkai (Symposium on Protein Structure, in Japanese)” pp. 37-40 (1992).
20. Koseki, T., Kitabatake, N., and Doi, E., Freezing denaturation of ovalbumin at acid pH. J. Biochem., 107, 389-394 (1990).
21. Tatsumi, E. and Hirose, M., Highly ordered molten globule-like state of ovalbumin at acidic pH: Native-like fragmentation by protease and selective modification of Cys367 with dithiopyri-dine. J. Biochem., 122, 300-308 (1997).
22. Nisbet, A. D., Saundry, R. H., Moir, A. J. G., Fothergill, L. A., and Fothergill, J. E., The complete amino-acid sequence of hen ovalbumin. Eur. J. Biochem., 115, 335-345 (1981).
23. Takahashi, N., Koseki, T., Doi, E., and Hirose, M., Role of intrachain disulfide bond in the conformation and stability of ovalbumin. J. Biochem., 109, 846-851 (1991).
24. Tatsumi, E., Takahashi, N., and Hirose, M., Denatured state of ovalbumin in high concentration of urea as evaluated by disulfide rearrangement analysis. J. Biol. Chem., 269, 28062-28067 (1994).
25. Corbett, R. J. T., and Roche, R. S., Use of high-speed size-exclusion chromatography for the study of protein folding and stability. Biochemistry, 23, 1888-1894 (1984).
26. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
27. Takahashi, N. and Hirose, M., Reversible denaturation of disulfide-reduced ovalbumin and its reoxidation generating the native cystine cross-link. J. Biol. Chem., 267, 11565-11572 (1994).
28. Onda, M., Tatsumi, E., Takahashi, N., and Hirose, M., Refolding of ureα-denatured ovalbumin that comprises non-native disulfide isomers. J. Biochem., 122, 83-89 (1997).
29. Onda, M., Tatsumi, E., Takahashi, N., and Hirose, M., Refolding process of ovalbumin from ureα-denatured state. Evidence for the involvement of nonproductive side chain interaction in an early intermediate. J. Biol. Chem., 272, 3973-3979 (1997).
30. Yun, T., Yamashita, H., Takahashi, N., and Hirose, M., Limited proteolysis of disulfide-reduced ovalbumin by subtilisin. Biosci. Biotechnol. Biochem., 57, 940-944 (1993).
31. Tatsumi, E., Yoshimatsu, D., and Hirose, M., Conformational state of ovalbumin at acidic pH as evaluated by novel approach utilizing intrachain sulfhydryl-mixed disulfide exchange reactions. Biochemistry, 37, 12351-12359 (1998).
32. Kraulis, P. J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystal-logr., 24, 946-950 (1991).