Non-dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3′,5′-AMP-stimulated protein kinase

Elisabet Humble, Lars Berglund, Vincent Titanji, Olle Ljungström, Bror Edlund, Örjan Zetterqvist, Lorentz Engström

Research output: Contribution to journalArticle

46 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)614-621
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume66
Issue number2
DOIs
StatePublished - Sep 16 1975
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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