Inactivation of Pyruvate Kinase Type M2from Chicken Liver by Phosphorylation, Catalyzed by a cAMP-Independent Protein Kinase
- 1 January 1977
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 358 (2) , 1047-1056
- https://doi.org/10.1515/bchm2.1977.358.2.1047
Abstract
A c[cyclic]AMP-independent protein kinase [EC 2.7.1.37] from chicken liver phosphorylated and inactivated pyruvate kinase [EC 2.7.1.40] type M2 from the same tissue. Complete inactivation was reached when 4 M of phosphate were incorporated/M of tetrameric pyruvate kinase. The protein kinase bound with high affinity to pyruvate kinase type M2 (Km value for pyruvate kinase = 6 .times. 10-10 M); it phosphorylated phosvitin and casein but not histones. ATP and GTP were substrates. The differences between the properties of this protein kinase in the interconversion of pyruvate kinase and that described previously were discussed.This publication has 22 references indexed in Scilit:
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