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  • Title: [Allosteric properties of muscle creatine kinase].
    Author: Chetverikova EP, Rozanova NA.
    Journal: Biokhimiia; 1977 Mar; 42(3):481-9. PubMed ID: 861308.
    Abstract:
    The dependence of the reaction rate on substrate concentrations at pH 8.0--7.5 does not submit the Michaelis-Menten kinetics. The dependence of v on Mg-ATP is described with a curve having an intermediate plateau. The dependence of v on the creatine concentration is expressed by a curve, which is not hyperbolic. In this case the index of the substrate concentration, (q), is variable, and it increases with the increase of creatine concentration from 1 to 2 (at the presence of effectors, PEP and ADP,--from 1 to 3.5). The specific creatine kinase activity increases 3--4-fold with protein dilution, but this effect is not observed in the presence of inhibitors to FDP and PEP. Creatine kinase is desensibilized with respect to FDP and PEP after a prolonged storage. The data obtained and the presence of an effector set indicate, that muscle creatine kinase is a regulated allosteric enzyme.
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