Read e-book online Control by Phosphorylation, Part A: General Features, PDF

By Paul D. Boyer, Edwin G. Krebs

ISBN-10: 0080865941

ISBN-13: 9780080865942

ISBN-10: 0121227170

ISBN-13: 9780121227173

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Extra info for Control by Phosphorylation, Part A: General Features, Specific Enzymes

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Because of an increase in sensitivity in this system, phosphorylation of the nanopeptide responds more sharply to increasing concentrations of CAMP than does the activation of the CAMP-dependent protein kinase. This apparent cooperativity derives from the fact that the catalytic subunit of the protein kinase forms a tight complex with the nanopeptide. Furthermore, in the presence of Pi, an inhibitor of the phosphatase, both the sensitivity and signal amplification were enhanced considerably (195).

224-240. 13. , and Murofushi, H. (1984). “Methods in Enzymology,” Vol. 106, pp. 223-237. 14. Huttner, W. B. (1984). “Methods in Enzymology,” Vol. 107, pp. 200-223. 15. Sutherland, E. , and Wosilait, W. D. (1955). Nature (London) 175, 169-170. 16. Fischer, E. , and Krebs, E. G. (1958). JBC 231, 65-71. 17. Holland, R . , Hardie, D. , Clegg, R. , and Zammit, V. A. (1985). BJ 226, 139-145. 18. -H. (1983). Curr. Top. Cell. Regul. 22, 143-176. 19. Davis, C. , Gordon, A. S . , and Diamond, I. (1982). PNAS 79, 3666-3670.

99, pp. 279-288. 97. Westwood, S. A,, Hudlicka, 0.. and Perry, S. V. (1984). BJ 218, 841-847. 98. Adelstein, R. S. (1983). J . Clin. Invest. 72, 1863-1866. 99. Costa, M. , Casnellie, J. , and Catterall, W. A. (1982). JBC 257, 7918-7921. 100. Mardh, S. (1983). Curr. Top. Membr. Trunsp. 19, 999-1004. 101. Atmar, V. , and Kuehn, G. D. (1983). “Methods in Enzymology,” Vol. 99, pp. 366-372. 102. Golf, S. , and Graef, V. (1984). J. Clin. Chem. Clin. Biochem. 22, 705-709. 103. , and Kaufman, S. (1978).

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Control by Phosphorylation, Part A: General Features, Specific Enzymes by Paul D. Boyer, Edwin G. Krebs


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