Study of regulatory properties of creatine kinase from white muscles of fishes
Taame, N.; Stefanov, V.E.; Lyzlova, S.N.
Biokhimiia 44(3): 460-466
1979
ISSN/ISBN: 0320-9725 PMID: 223669 Document Number: 143615
The kinetic and regulatory properties of creatine kinase from Silurus glanis L. white muscles were studied. The effects of several glycolytic intermediates, AMP and pyrophosphate on the creatine kinase reaction catalyzed by fresh and aged enzyme preparations were studied. Glucose-6-phosphate, fructose-1,6-diphosphate, phosphoenolpyruvated and AMP were shown to inhibit the creatine kinase reaction, increasing the cooperativity of the substrate binding. Pyrophosphate exerted a two-phase effect (activation and inhibition) in case of fresh enzyme preparations and one-phase effect (inhibition) in case of aged ones.