Abstract
The soluble cyclic AMP-dependent protein kinase of bovine heart has been purified to homogeneity. It is an asymmetric protein with a molecular weight of 174,000 and is composed of two globular catalytic subunits (molecular weight, 38,000) and an asymmetric cyclic nucleotide-binding protein (molecular weight, 98,000). The cyclic AMP-binding protein consists of two polypeptide chains of equal size and is able to serve as substrate for a protein kinase-catalyzed phosphotransferase reaction. The physiological significance of this “autophosphorylation” of protein kinase has not been established. The protein kinase activity associated with the plasma membrane of the human erythrocyte has many properties in common with soluble protein kinases including the ability to be dissociated into cyclic AMP-independent kinase and cyclic AMP-binding activities. Membrane-bound protein kinase catalyzes the phosphorylation of three endogenous membrane proteins, two of them in a cyclic nucleotide-dependent fashion. Both the cyclic AMP-binding and phosphotransferase activities of the human erythrocyte membrane appear to be localized on the inner cytoplasmic surface of the membrane.
Supported by grants from the National Institutes of Health (AM09038) and American Cancer Society (BC-12B). O.M.R. is a recipient of a Career Development Award from the USPHS, J.E. is a fellow of the Muscular Dystrophy Assns. of America and C.S.R. is a career scientist of the Health Research Council of N.Y.C.
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Rosen, O.M., Erlichman, J., Rubin, C.S. (1974). Molecular Characterization of Cyclic AMP-Dependent Protein Kinases Derived from Bovine Heart and Human Erythrocytes. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_14
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DOI: https://doi.org/10.1007/978-3-642-80817-3_14
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