High salt concentrations induce dissociation of dimeric rabbit muscle creatine kinase. Physico-chemical characterization of the monomeric species

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1339, Issue 2, 1997, Pages 277-288

  Couthon, Fabienne ^b   Clottes, Eric ^b   Vial, Christian ^a,b  

^a UNIVERSITÉ LYON 1   (France)

^b UNIVERSITÉ LYON 1   (France)

Author keywords

Chemical modification; Dissociation; Inactivation; Intermediate state; Unfolding

Indexed keywords

CREATINE KINASE; CREATINE KINASE MM; SODIUM CHLORIDE;

ANIMAL TISSUE; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STRUCTURE; MUSCLE; NONHUMAN; PRIORITY JOURNAL; RABBIT;

ANIMALS; BINDING SITES; CREATINE KINASE; DIMERIZATION; LITHIUM CHLORIDE; MUSCLE, SKELETAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RABBITS; SALINE SOLUTION, HYPERTONIC;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0030951344     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(97)00010-1     Document Type: Article

References (29)

1. Marcillat, O., Goldschmidt, D., Eichenberger, D. and Vial, C. (1987) Biochim. Biophys. Acta 890, 233-241.
2. Putney, S., Herlihy, W., Royal, N., Pang, H., Vasken Aposhian, H., Pickering, L., Belagaje, R., Biemann, K., Page, D., Kuby, S. and Schimmel, P. (1984) J. Biol. Chem. 259, 14317-14320.
3. Fritz-Wolf, K., Schnyder, T., Wallimann, T. and Kabsch, W. (1996) Nature 381, 341-345.
4. Mühlebach, S.M., Gross, M., Wirz, T., Wallimann, T., Perriard, J.C. and Wyss, M. (1994) Mol. Cell. Biochem. 133/134, 245-262.
5. Morris, G.E. and Jackson, P.J. (1991) Biochem. J. 280, 809-811.
6. Gross, M., Wyss, M., Furter-Graves, E.M., Wallimann, T. and Furter, R. (1996) Prot. Sci. 5, 320-330.
7. Mahowald, T.A., Noltmann, E.A. and Kuby, S.A. (1962) J. Biol. Chem. 237, 1535-1548.
8. Price, N.C. (1979) Biochem. J. 177, 603-612.
9. Messmer, C.H. and Kägi, H.R. (1985) Biochemistry 24, 7172-7178.
10. Gross, M., Furter-Graves, E.M., Wallimann, T., Eppenberger, H.M. and Furter, R. (1994) Prot. Sci. 3, 1058-1068.
11. Clottes, E. and Vial, C. (1996) Arch. Biochem. Biophys. 329, 97-103.
12. Couthon, F., Clottes, E., Ebel, C. and Vial, C. (1995) Eur. J. Biochem. 234, 160-170.
13. Gross, M., Lustig, A., Wallimann, T. and Furter, R. (1995) Biochemistry 34, 10350-10357.
14. Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F. and Gilmanshin, R.I. (1991) Biopolymers 31, 119-128.
15. Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) J. Biol. Chem. 193, 265-275.
16. Bensadoun, A. and Weinstein, D. (1976) Anal. Biochem. 70, 241-250.
17. Font, B., Vial, C., Goldschmidt, D., Eichenberger, D. and Gautheron, D.C. (1981) Arch. Biochem. Biophys. 2121, 195-203.
18. Clottes, E., Couthon, F., Denoroy, L. and Vial, C. (1994) Biochim. Biophys. Acta 1209, 171-176.
19. Schägger, H. and von Jagow, G. (1987) Anal. Biochem. 166, 368-379.
20. Le Maire, M., Aggerbeck, L.P., Monteilhet, C., Andersen, J.P. and Moller, J.V. (1986) Anal. Biochem. 154, 525-535.
21. Uversky, V.N. (1993) Biochemistry 32, 13288-13298.
22. McLaughlin, A.C. (1974) J. Biol. Chem. 249, 1445-1452.
23. Garwonski, T.H. and Westhead, E.W. (1969) Biochemistry 8, 4261-4270.
24. Keresztes-Nagy, S. and Orman, R. (1971) Biochemistry 10, 2506-2508.
25. Kornblatt, M.J., Al-Ghanim, A. and Kornblatt, J.A. (1996) Eur. J. Biochem. 236, 78-84.
26. Mahowald, T.A. (1969) Fed. Proc. 28, 601.
27. Jacobson, G.R., Schaffer, M.H., Stark, G.R. and Vanaman, T.C. (1973) J. Biol. Chem. 248, 6583-6591.
28. Arakawa, T. and Timasheff, S.N. (1982) Biochemistry 21, 6545-6552.
29. Grossman, S.H., Pyle, J. and Steiner, R.J. (1981) Biochemistry 20, 6122-6128.