Structure, regulation, denaturation of rabbit muscle glycogen phosphorylase b

Biochemistry (Moscow)

Volumn 61, Issue 11, 1996, Pages 1432-1442

  Livanov, N B ^a   Kornilaev, B A ^a  

^a BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

Author keywords

Allosteric regulation; Denaturation; Glycogen phosphotylase; Protein structure; Thermal stability

Indexed keywords

ORYCTOLAGUS CUNICULUS;

EID: 0000470434     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (80)

1. Parnas, J. K., and Baranowski, T. (1935) Compt. Rend. Soc. Biol., 120, 307-311.
2. Parnas, J. K. (1936) Compt. Rend. Soc. Biol., 121, 282-285.
3. Cori, C. F., and Cori, G. T. (1936) Proc. Soc. Exp. Biol. Med, 34, 202-205.
4. Cori, G. T., Colowick, S. P., and Cori, C. F. (1938) J. Biol. Chem., 123, 381-389.
5. Cori, G. T., and Cori, C. F. (1945) J. Biol. Chem., 158, 324-332.
6. Madsen, N. B., and Cori, C. F. (1956) J. Biol. Chem., 223, 1055-1066.
7. Wang, J. H., Shonka, M. L., and Graves, D. J. (1965) Biochemistry, 4, 2296-2301.
8. Krebs, E. G., and Fischer, E. H. (1956) Biochim. Biophys. Acta, 20, 150-156.
9. Graves, D. J., Fischer, E. H., and Krebs, E. G. (1960) J. Biol. Chem., 235, 805-809.
10. Graves, D. J., and Wang, J. H. (1972) in The Enzymes (Boyer, P. D., ed.) Academic Press, New York, Vol. 7, pp. 435-482.
11. Lissovskaya, N. P., and Livanova, N. B. (1975) in Biological Chemistry. Allosteric Enzymes (V. L. Kretovich, ed.) [in Russian], VIN-ITI, Moscow, Vol. 8, pp. 110-163.
12. Dombradi, V. (1981) Int. J. Biochem., 13, 125-139.
13. Oikonomakos, N. G., Acharya, K. R., and Johnson, L. N. (1992) in Post-Translational Modifications of Proteins (Harding, J. J., and Crabbe, M. J. C., eds.) CRS Press, Boca Raton, pp. 81-150.
14. Kurganov, B. I. (1995) in Proteins and Peptides (Ivanov, V. T., and Lipkin, V. M., eds.) [in Russian], Nauka, Moscow, pp. 109-117.
15. Morgan, H. E., and Parmeggiani, A. (1964) J. Biol. Chem., 239, 2440-2445.
16. Okazaki, T., Nakazawa, A., and Hayashi, O. (1968) J. Biol. Chem., 243, 5266-5271.
17. Silonova, G. V., and Lissovskaya, N. P. (1967) Dokl. Akad. Nauk SSSR, 174, 713-720.
18. Klinov, S. V., Chebotareva, N. A., Kurganov, B. I., Litvak, Zh. I., Zhilina, T. A., Glebova, G. D., Pekel', N. D., and Berezovskii, V. M. (1984) Bioorg. Khim., 10, 1161-1170.
19. Cori, G. T., Colowick, S. P., and Cori, C.F. (1939) J. Biol. Chem., 127, 771-782.
20. Kasvinsky, P. J., Madsen, N. B., and Fletterick, R. J. (1978) J. Biol. Chem., 253, 1290-1296.
21. Krebs, E. G. (1954) Biochim. Biophys. Acta, 15, 508-515.
22. Madsen, N. B., and Cori, C. F. (1954) Biochim. Biophys. Acta, 15, 516-521.
23. Wang, J. H., Humniski, P., and Black, W. J. (1968) Biochemistry, 7, 2037-2044.
24. Cohen, P., Duewer, T., and Fischer, E. H. (1971) Biochemistry, 10, 2683-2694.
25. Silonova, G. V., and Kurganov, B. I. (1970) Mol. Biol. (Moscow), 4, 445-459.
26. Huang, C. Y., and Graves, D. J. (1970) Biochemistry, 9, 660-671.
27. Feldmann, K., Zeisel, H., and Helmreich, E. (1972) Proc. Natl. Acad. Sci. USA, 69, 2278-2282.
28. Titani, K., Koide, A., Hermann, J., Ericsson, L. H., Kumar, S., Wade, R. D., Walsh, K. A., Neurath, H., and Fischer, E. H. (1977) Proc. Natl. Acad. Sci. USA, 74, 4762-4766.
29. Nakano, K., Hwang, P. K., and Fletteric, R. J. (1986) FEBS Lett., 204, 283-287.
30. Barford, D., and Johnson, L. N. (1992) Protein Sci., 1, 472-493.
31. Johnson, G. F., Tu, J. I., Bartlett, M. L., and Graves, D. J. (1970) J. Biol. Chem. 245, 5560-5568.
32. Klein, H. W., Im, M. J., Palm, D., and Helmreich, E. J. M. (1984) Biochemistry, 23, 5853-5861.
33. Johnson, L. N., and Barford, D. (1990) J. Biol. Chem., 265, 2409-2412.
34. Johnson, L. N., Snape, P., Martin, J. L., Acharya, K. R., Barford, D., and Oikonomakos, N. G. (1993) J. Mol. Biol., 232, 253-267.
35. Dawson, M. J., Gadian, D. G., and Wilkie, D. R. (1980) J. Physiol., 299, 465-484,
36. Barford, D., and Johnson, L. N. (1989) Nature, 340, 609-616.
37. Kasvinsky, P. J., Shechosky, S., and Fletteric, R. J. (1978) J. Biol. Chem., 253, 9102-9106.
38. Sprang, S., Fletterick, R., Stern, M., Yang, D., Madsen N. B., and Sturtevant, J. (1982) Biochemistry, 21, 2036-2048.
39. Meyer, F., Heilmeyer, L. M. G., Jr., Haschke, R. H., and Fischer, E. H. (1970) J. Biol. Chem., 245, 6642-6648.
40. Fischer, E. H., Graves, D. J., Crittenden, E. R. S., and Krebs, E. G. (1959) J. Biol. Chem., 234, 1698-1704.
41. Hurd, S. S., Teller, D., and Fischer, E. H. (1966) Biochem. Biophys. Res. Commun., 24, 79-84.
42. Bot, G., Kovacs, E., and Gergely, P. (1974) Biochim. Biophys. Acta, 370, 70-74.
43. Livanova, N. B., Eronina, T. B., and Silonova, G. V. (1972) FEBS Lett., 24, 82-84.
44. Madsen, N. B. (1986) in The Enzymes (Boyer, P. D., and Krebs, E. G., eds.) Academic Press, New York, Vol. 17, pp. 366-394.
45. Helmreich, E., Michaelides, M. C., and Cori, C. F. (1967) Biochemistry, 6, 3695-3710.
46. Buc, H. (1967) Biochem. Biophys. Res. Commun., 28, 59-64.
47. Black, W.J., and Wang, J.H. (1968) J. Biol. Chem., 243, 5892-5898.
48. Helmreich, E., and Con, C. F. (1964) Proc. Natl. Acad. Sci. USA, 51, 131-138.
49. Madsen, N. B., and Shechosky, Sh. (1967) J. Biol. Chem., 242, 3301-3307.
50. Silonova, G. V., Livanova, N. B., and Kurganov, B. I. (1970) Mol. Biol. (Moscow), 3, 768-784.
51. Klinov, S. V., and Kurganov, B. I. (1994) Biochemistry (Moscow), 59, 629-637.
52. Sansom, M. S., Stuart, D. J., Acharya, K. R., Hajdu, J., McLaughlin, P. J., and Johnson, L. N. (1985) J. Mol. Struct., 123, 3-25.
53. Sprang, S. R., Withers, S. G., Goldsmith, E. J., Fletteric, R. J., and Madsen, N. B. (1991) Science, 254, 1367-1371.
54. Kastenschmidt, L. L., Kastenschmidt, J., and Helmreich, E. (1968) Biochemistry, 7, 4543-4556.
55. Feldmann, K., and Hull, W. E. (1977) Proc. Natl. Acad. Sci. USA, 74, 836-860.
56. Mott, D. M., and Bieber, A. L. (1970) J. Biol. Chem., 245, 4058-4066.
57. Barford, D., Hu, S.-H., and Johnson, L. N. (1991) J. Mol. Biol., 218, 233-260.
58. Kiselev, N. A., Lerner, F. Y., and Livanova, N. B. (1971) J. Mol. Biol., 62, 537-549.
59. Tessmer, G. W., Skuster, J. R., Tabatabai, L. B., and Graves, D. J. (1977) J. Biol. Chem., 252, 5666-5671.
60. Luo, S., Martin, B. L., Senshu, T., and Graves, D. J. (1995) Arch. Biochem. Biophys., 318, 362-369.
61. Eronina, T. B., Livanova, N. B., Chebotareva, N. A., Kurganov, B. I. Luo, S., and Graves, D. J. (1994) Mol. Biol. (Moscow), 28, 841-847.
62. Rogers, G. E. (1962) Nature, 194, 1149-1151.
63. Kurganov, B. I., Shchors, E. I., Chebotareva, N. A., and Klinov, S. V. (1995) Biochemistry (Moscow), 60, 61-72.
64. Calder, P. C. (1991) Int. J. Biochem., 23, 1335-1352.
65. Jaenicke, R., and Rudolph, R. (1986) Meth. Enzymol., 131, 218-250.
66. Kastenschmidt, L. L., Kastenschmidt, J., and Helmreich, E. (1968) Biochemistry, 7, 3590-3607.
67. Ullmann, A., Goldberg, M. E., Perrin, D., and Monod, J. (1968) Biochemistry, 7, 261-265.
68. Seery, V. L., Fischer E. H., and Teller, D. C. (1970) Biochemistry, 9, 3591-3598.
69. Shaltiel, Sh., Hedrick, J. L., and Fischer E. H. (1966) Biochemistry, 5, 2108-2117.
70. Hedrick, J. L., Smith, A. J., and Bruening, G E. (1969) Biochemistry, 8, 4012-4019.
71. Livanova, N. B., Pikhelgas, V. Ya., and Shpikiter, V. O. (1965) Dokl. Akad. Nauk SSSR, 161, 1222-1223.
72. Tu, G.-Ch., and Tsou, C.-L. ( 1965) Acta Biochim. Biophys. Sinica, 5, 599-606.
73. Hedrick, J. L., Shaltiel, Sh., and Fischer, E. H. (1966) Biochemistry, 5, 2117-2125.
74. Sugrobova, N. P., Lissovskaya, N. P., and Kurganov, B. I. (1982) Biokhimiya, 47, 1883-1888.
75. Kornilaev, B. A., Kurganov, B. I., Eronina, T. B., and Livanova, N. B. (1996) Biochemistry (Moscow), 61, 628-634.
76. Kornilaev, B. A., Kurganov, B. I., Eronina, T. B., and Livanova, N. B. (1996) Biochem. Mol. Biol. Int., 38, 921-927.
77. Kornilaev, B. A., Kurganov, B. I., Eronina, T. B., Chebotareva, N. A., Livanova, N. B., Orlov, V. N., and Chernyak, V. Ya. (1997) Mol. Biol. (Moscow), in press.
78. Lumry, R., and Eyring, E. (1954) J. Phys. Chem., 58, 110-120.
79. Ptitsyn, O. V. (1995) Trends Biochem. Sci., 20, 376-379.
80. Centeno, F., Fernandez-Salquero, P., Laynez, L. L., and Gutierrez-Merino, G. (1992) J. Bioenerg. Biomembr., 24, 625-634.