Change in kinetic regime of protein aggregation with temperature increase. Thermal aggregation of rabbit muscle creatine kinase

Biochemistry (Moscow)

Volumn 71, Issue 3, 2006, Pages 325-331

  Fedurkina, N V ^a   Belousova, L V ^b   Mitskevich, L G ^a   Zhou, H M ^c   Chang, Z ^d   Kurganov, B I ^a  

^a BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c TSINGHUA UNIVERSITY   (China)

^d PEKING UNIVERSITY   (China)

Author keywords

Creatine kinase; Kinetics; Small heat shock protein Hsp 16.3; Thermal aggregation

Indexed keywords

BACTERIA; DIFFERENTIAL SCANNING CALORIMETRY; GROWTH (MATERIALS); MUSCLE; REACTION KINETICS;

CREATINE KINASE; KINETICS; SMALL HEAT SHOCK PROTEIN HSP 16.3; THERMAL AGGREGATION;

ENZYMES;

MYCOBACTERIUM TUBERCULOSIS; ORYCTOLAGUS CUNICULUS;

BACTERIAL PROTEIN; CHAPERONIN; CREATINE KINASE; HSP16.3 PROTEIN, MYCOBACTERIUM TUBERCULOSIS;

ANIMAL; ARTICLE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; HEAT; METABOLISM; PROTEIN DENATURATION; RABBIT; SKELETAL MUSCLE; THERMODYNAMICS;

ANIMALS; BACTERIAL PROTEINS; CHAPERONINS; CREATINE KINASE; ENZYME STABILITY; HEAT; MUSCLE, SKELETAL; PROTEIN DENATURATION; RABBITS; THERMODYNAMICS;

EID: 33645282235     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S000629790603014X     Document Type: Article

References (40)

1. Fink, A. L. (1998) Folding and Design, 3, R9-R23.
2. Jaenicke, R. (1995) Philos. Trans. R. Soc. Lond. B. Biol. Sci., 348, 97-105.
3. Kurganov, B. I. (2002) Biochemistry (Moscow), 67, 409-422.
4. Kurganov, B. I. (2002) Uspekhi Biol. Khim., 42, 89-138.
5. Markossian, K. A., and Kurganov, B. I. (2004) Biochemistry (Moscow), 69, 971-984.
6. Prusiner, S. B. (1998) Proc. Natl. Acad. Sci. USA, 95, 13363-13383.
7. Moriachi, M., and Caughey, G. (1999) Structure, 7, R231-R240.
8. Gusev, N. B., Bogatcheva, N. V., and Marston, S. B. (2002) Biochemistry (Moscow), 67, 511-519.
9. Panasenko, O. O., Kim, M. B., and Gusev, N. B. (2003) Uspekhi Biol. Khim., 43, 59-98.
10. Bai, J.-H., Zheng, S.-Y., and Zhou, H.-M. (1998) Biochem. Mol. Biol. Int., 45, 941-951.
11. Lyubarev, A. E., Kurganov, B. I., Orlov, V. N., and Zhou, H.-M. (1999) Biophys. Chem., 35, 7895-7902.
12. Meng, F.-G., Hong, Y.-K., He, H.-W., Lyubarev, A. E., Kurganov, B. I., Yan, Y-B., and Zhow, H.-M. (2004) Biophys. J., 87, 2247-2257.
13. Chen, L. H., Borders, Ch. L., Jr., Vasquez, J. R., and Kenyon, G. L. (1996) Biochemistry, 35, 7895-7902.
14. Cox, J. M., Davis, C. A., Chan, Ch., Jourden, M. J., Jorjorian, A. D., Brym, M. J., Snider, M. J., Borders, Ch. L., Jr., and Edmiston, P. L. (2003) Biochemistry, 42, 1863-1871.
15. Couthon, F., Clottes, E., and Vial, C. (1996) Biochem. Biophys. Res. Commun., 227, 854-860.
16. Watts, D. C. (1973) in The Enzymes (Boyer, P. I., ed.) Vol. 8, pp. 383-455.
17. Kenyon, G. L., and Reed, G. H. (1983) Adv. Enzymol., 54, 367-426.
18. Dawson, M., Eppenberger, H. M., and Kaplan, N. O. (1967) J. Biol. Chem., 242, 210-216.
19. Walliman, T., Wyss, M., Brdiczka, D., Nicolay, K., and Eppenberger, H. M. (1992) Biochem. J., 281, 21-40.
20. Kuby, S. A., Noda, L., and Lardy, H. A. (1954) J. Biol. Chem., 209, 191-201.
21. Kuby, S. A., Noda, L., and Lardy, H. A. (1954) J. Biol. Chem., 210, 65-71.
22. Rao, J. K. M., Bujacz, G., and Wlodawer, A. (1998) FEBS Lett., 439, 133-137.
23. Fritz-Wolf, K., Schnyder, T., Wallimann, T., and Kabson, W. (1996) Nature, 381, 341-345.
24. Leydier, C., Clottes, E., Couthon, F., Marcillat, O., Ebel, C., and Vial, C. (1998) Biochemistry, 37, 17579-17589.
25. Kuznetsova, I. M., Stepanenko, O. V., Turoverov, K. K., Zhu, L., Zhou, J.-M., Fink, A. L., and Uverssky, V. N. (2002) Biochim. Biophys. Acta, 1396, 138-155.
26. Chang, Z., Primm, T. P., Jakana, J., Lee, I. H., Serysheva, I., Chiu, W, Gilbert, H. F., and Quicho, F. A. (1996) J. Biol. Chem., 271, 7218-7223.
27. Gu, L., Abulimiti, A., Li, W., and Chang, Z. (2002) J. Mol. Biol., 319, 517-526.
28. Abulimiti, A., Fu, X., Gu, L., Chen, X., and Chang, Z. (2003) J. Mol. Biol., 326, 1013-1023.
29. Fu, X., Jiao, W, Abulimiti, A., and Chang, Z. (2004) Biochemistry (Moscow), 69, 552-557.
30. Fu, X., and Chang, Z. (2004) Biochem. Biophys. Res. Commun., 316, 291-299.
31. Chen, X., Fu, X., Ma, Y., and Chang, Z. (2005) Biochemistry (Moscow), 70, 913-919.
32. Yao, Q. Z., Zhou, H. M., Hou, L. Z., and Tsou, C. L. (1982) Sci. Sin.,26B, 1296-1302.
33. Noda, L., Kuby, S. A., and Lardy, H. (1954) Meth. Enzymol., 2, 605-610.
34. Wood, T. D., Guan, Z., Borders, C. L., Jr., Chen, L. H., Kenyon, G. L., and McLafferty, F. W. (1998) Proc. Natl. Acad. Sci. USA, 95, 3362-3365.
35. Kurganov, B. I., Dobrov, E. N., Rafikova, E. R., Fedurkina, N. V., Mitskevich, L. G., Belousova, L. V., and Zhou, H.-M. (2001) Proc. 1st Tsinghua Int. Conf. of Protein Sciences (TIPCPS), Tsinghua University, Beijing, China, p. 36.
36. Kurganov, B. I., Rafikova, E. R., and Dobrov, E. N. (2002) Biochemistry (Moscow), 67, 525-533.
37. Rafikova, E. R., Kurganov, B. I., Arutyunyan, A. M., Kust, S. V., Drachev, V. A., and Dobrov, E. N. (2003) Int. J. Biochem. Cell Biol., 1508, 1-9.
38. Wang, K., and Kurganov, B. I. (2003) Biophys. Chem., 106, 97-109.
39. Patro, S. Y., and Przybycien, T. M. (1996) Biophys. J., 70, 2888-2902.
40. Kurganov, B. I. (1998) Biochemistry (Moscow), 63, 364-367.