title: [Allosteric properties of muscle creatine kinase].
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.
mesh_terms: D000244:Adenosine Diphosphate; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D000494:Allosteric Regulation; D000818:Animals; D002384:Catalysis; D003401:Creatine; D003402:Creatine Kinase / Q000037:antagonists & inhibitors; D007700:Kinetics; D008274:Magnesium; D009132:Muscles / Q000201:enzymology*; D010728:Phosphoenolpyruvate; D011817:Rabbits
chemical_list: D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D000255:Adenosine Triphosphate; D003402:Creatine Kinase; D008274:Magnesium; D003401:Creatine
vernacular_title: Allostericheskie svoĭstva myshechnoĭ kreatinkinazy