@article{793a6949df6b4328bbebe9e97212fadc,
title = "[44] Cyclic AMP-Dependent Protein Kinase from Bovine Heart Muscle",
abstract = "Cyclic AMP (cAMP)-dependent protein kinase catalyzes the transfer of the γ-phosphate of ATP to serine or threonine hydroxyl groups in various protein substrates. The addition of cAMP greatly enhances the velocity of the phosphotransferase reaction. The activity of the enzyme is determined by measuring the amount of 32P transferred from [γ-32P] ATP to protamine or histone. The labeled protein substrate is separated from the assay mixture by precipitation with trichloroacetic acid and collected on glass fiber filters. Assays are carried out in the presence and absence of cAMP to evaluate the activation of the enzyme by the cyclic nucleotide. One unit of protein kinase activity is defined as that amount of enzyme necessary to catalyze the transfer of 1 nmole of 32P from [γ-32P] ATP to protamine per minute at 30°C. A unit of binding activity is equivalent to the binding of 1 nmole of cAMP. Specific activity is expressed as units per milligram of protein.",
author = "Rubin, {Charles S.} and Jack Erlichman and Rosen, {Ora M.}",
note = "Funding Information: The action of a wide variety of hormones has been shown by Sutherland and his associates 2 to be mediated by adenosine 3',5'-cyclic monophosphate (cAMP). In rabbit skeletal muscle, a cAMP-dependent protein kinase which catalyzes the phosphorylation and activation of phosphorylase b kinase has been isolated by Walsh et al. ~ Thus one of the links in the sequence of reactions between hormonal stimulation of adenylate cyclase and increased glycogenolysis in muscle has been identified. Since the initial report, the occurrence of cAMP-dependent protein kinases has been shown to be widespread. 4-7 '\]?hea ction of these enzymes is found to be relatively nonspecific; several proteins, such as histone, protamine, casein, may also serve as substrates. The presence of multiple forms of protein kinase was first demonstrated in rabbit red blood cells 7 and, subsequently, was also found in other tissues. ~-1~ 1T his work was supported in part by grants from the American Cancer Society (BC-65 and BC-85A) and from the National Science Foundation (GB 27435 A#1). The author is an Established Investigator of the American Heart Association. 2 G. A. Robison, R. W. Butcher, and E. W. Sutherland, {"}Cyclic AMP.{"} Academic Press, New York, 1971. a D. A. Walsh, J. P. Perkins, and E. G. Krebs, \]. Biol. Chem. 243, 3763 (1968). T. A. Langan, Science 169., 579 (1968). 5j . F. Kuo and P. Greengard, Proc. Nat. Acad. Sci. U.S. 64, 1349 (1969). ~ff. D. Corbin and E. G. Krebs, Biochem. Biophys. Res. Commun. 36, 328 (1969). 7M . Tao, M. L. Salas, and F. Lipmann, Proc. Nat. Acad. Sci. U.S. 67, 408 (1970). s E. M. Reimann, D. A. Walsh, and E. G. Krebs, J. Biol. Chem. 246, 1986 (1971). ~A. Kumon, K. Nishiyama, H. Yamamura, and Y. Nishizuka. J. Biol. Chem. 247, 3726 (1972). ~ F. Lipmann, Advan. Enzyme Regul. 9, 5 (1971).",
year = "1974",
month = jan,
day = "1",
doi = "10.1016/0076-6879(74)38047-0",
language = "English (US)",
volume = "38",
pages = "308--315",
journal = "Methods in enzymology",
issn = "0076-6879",
publisher = "Academic Press Inc.",
number = "C",
}