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The magnesium dependent atpase from the erythrocyte plasma membrane of the flounder platichthys flesus general properties and some observations on the steady state kinetics


, : The magnesium dependent atpase from the erythrocyte plasma membrane of the flounder platichthys flesus general properties and some observations on the steady state kinetics. Comparative Biochemistry & Physiology B 75(1): 153-162

The plasma membrane of the flounder erythrocyte contains a Mg2+-dependent ATPase which is insensitive to ouabain Mg2+ is part of the substrate, Mg-ATP, and Mg2+ also functions as a nonessential activator. Ca2+, Mn2+ and Co2+ can replace Mg2+ as an activator of ATP hydrolysis. Cu2+ and Zn2+ abolish the Mg-dependent activity. Ca2+ and Mg2+ activate the same enzyme and Mg-ATP and Ca-ATP are mutually competitive. The hydrolysis of ATP obeys Michaelis-Menten kinetics whether or not the Mg2+-ATPase is fully activated by Mg2+. The Km values for Mg-ATP were 0.13 and 0.43 mM respectively. Free ATP acts as a competitive inhibitor towards Mg-ATP and the dissociation constant for the enzyme-ATP complex was .apprx. 0.55 mM. The Mg2+-ATPase has a low specificity and reacts with GTP, ITP, UTP and CTP. The enzyme has a broad pH optimum ranging from 6.5-7.2 and an energy of activation of 13.5 kcal/mol between 0.degree.-30.degree. C. The effect of some activators and inhibitors of membrane-bound ATPases are reported.

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