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• W1537719062 endingPage "8153" @default.
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• W1537719062 abstract "Abstract An endogenous adenosine 3',5'-monophosphate-dependent protein kinase that catalyzes the phosphorylation of an endogenous protein in extensively washed human erythrocyte ghosts has been studied. This system is unique in that it has been possible to determine many of the properties of this membrane-associated enzyme using its endogenous protein substrate instead of an added exogenous phosphate acceptor such as histone. In the presence of adenosine 3',5'-monophosphate (cyclic AMP) and [γ-32P]ATP maximum incorporation of 32P]phosphate was observed at pH 6.5. The concentration of cyclic AMP that gave one-half maximal stimulation was 0.23 µm. Other cyclic nucleotides would maximally stimulate [32P]phosphate incorporation but at much higher concentrations. The nucleoside triphosphates, GTP, UTP, and CTP, reduced the amount of [32P]phosphate incorporated from [γ-32P]ATP in the presence of cyclic AMP and in its absence. The divalent cation, Mg2+, was required for activity, and in the presence of Ca2+ the enzyme was strongly inhibited. A cyclic AMP-binding protein also was present in extensively washed human erythrocyte ghosts. In the presence of Mg2+ the apparent dissociation constant for cyclic AMP was 3.3 nm. Fractionation of 32P-labeled human erythrocyte ghosts revealed that cyclic AMP stimulated incorporation into the protein fraction. Polyacrylamide gel electrophoresis of solubilized 32P-labeled human erythrocyte ghosts showed that the phosphorylation of one or two classes of proteins was specifically increased in the presence of cyclic AMP." @default.
• W1537719062 created "2016-06-24" @default.
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• W1537719062 date "1972-12-01" @default.
• W1537719062 modified "2023-10-16" @default.
• W1537719062 title "Phosphorylation of an Endogenous Membrane Protein by an Endogenous, Membrane-associated Cyclic Adenosine 3′,5′-Monophosphate-dependent Protein Kinase in Human Erythrocyte Ghosts" @default.
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• W1537719062 doi "https://doi.org/10.1016/s0021-9258(20)81821-3" @default.
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