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- W2072613590 abstract "1.|Four fractions of protein kinase (EC 2.7.1.37) activity (Peak IH, IIH, IIIC and IVC) have been resolved and partially purified from the 100 000 × g supernatant fraction of bovine parotid glands by DEAE-cellulose and phosphocellulose chromatographies. 2.|The protein kinases of Peak IH and IIH were adenosine 3′,5′-monophosphate (cyclic AMP)-dependent and had similar enzymic properties. The enzyme activities of Peak IIIC and IVC were cyclic-AMP independent, but there were some distinct differences between their properties. The protein kinase in Peak IIIC was activated by 0.2 M NaCl or KCl and phosphorylated casein preferentially as the substrate, utilizing only ATP as a phosphate donor. On the other hand, the protein kinase in Peak IVC was inhibited by univalent salts and preferred phosvitin to casein, utilizing either ATP or GTP as a phosphate donor. 3.|Tolbutamide increased the Km value for ATP and the dissociation constant for cyclic AMP, resulting in the inhibition of cyclic-AMP dependent protein kinase activity in the presence of cyclic AMP. Tolbutamide and its carboxy derivative, 1-butyl-3-p-carboxyphenylsulfonylurea, exerted almost no inhibitory effect on either the cyclic-AMP dependent protein kinase activities in the absence of cyclic AMP or on the cyclic-AMP independent protein kinase activities." @default.
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- W2072613590 date "1976-03-01" @default.
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- W2072613590 title "Characterization of protein kinases from bovine parotid glands The effect of tolbutamide and its derivative on these partially purified enzymes" @default.
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- W2072613590 doi "https://doi.org/10.1016/0005-2744(76)90037-1" @default.
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