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- W1967175090 abstract "Alkali-inactivated pig liver pyruvate kinase, type L, and a cyanogen bromide fragment from the same enzyme were shown to be phosphorylated by (32P)ATP and cyclic 3′,5′-AMP-stimulated protein kinase. In both cases the rate of phosphorylation was higher than with the native enzyme. Pyruvate kinases types A and M were not phosphorylated under the same conditions. From the 32P-labelled cyanogen bromide fragment (32P)phosphorylserine was isolated. The electrophoretic pattern of (32P)phosphopeptides obtained on partial acid hydrolysis of the fragment indicated that the phosphorylated site of the fragment was identical with that of the native pyruvate kinase." @default.
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- W1967175090 date "1975-09-01" @default.
- W1967175090 modified "2023-09-26" @default.
- W1967175090 title "Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3′,5′-AMP-stimulated protein kinase" @default.
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- W1967175090 doi "https://doi.org/10.1016/0006-291x(75)90554-9" @default.
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