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Regulation by phosphorylation-dephosphorylation of pyruvate kinase in Venus gallina and Scapharca inaequivalvis

Authors :
Emilio Carpene
Gloria Isani
G. Hakim
P. Cortesi
Source :
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 80:109-112
Publication Year :
1985
Publisher :
Elsevier BV, 1985.

Abstract

1. 1. Pyruvate kinase from the posterior adductor muscle of bivalve molluscs Venus gallina and Scapharca inaequivalvis can be converted into a more active form by treatment with a cyclic AMP-dependent protein kinase. 2. 2. The enzyme from Scapharca is inhibited through incubation with a non-specific phosphatase. 3. 3. Purified pyruvate kinase from Venus treated with protein kinase is affected by alanine in a way similar to the untreated enzyme. 4. 4. Phosphorylation is thought to be an additional mechanism of regulation of pyruvate kinase in anaerobiosis and under gluconeogenetic conditions.

Details

ISSN :
03050491
Volume :
80
Database :
OpenAIRE
Journal :
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry
Accession number :
edsair.doi...........54e526e94258a4ad6c72d492a8a6ee44