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  • Title: [Catalytic properties of purified Ca2+,Mg2+-ATPase from the myometrium sarcolemma].
    Author: Liubakovskaia LA, Slinchenko NN, Burchinskaia NF, Kurskiĭ MD.
    Journal: Biokhimiia; 1990 Jul; 55(7):1237-43. PubMed ID: 2145982.
    Abstract:
    The catalytic properties of myometrium sarcolemmal Ca2+, Mg2(+)-ATPase purified from plasma membrane solubilizate by affinity chromatography on calmodulin-Sepharose were investigated. The enzyme isolated in the presence of azolectin revealed a calmodulin-independent affinity for Ca2+ (Km = 0.17 microM). Purified Ca2+, Mg2(+)-ATPase displayed a strict substrate specificity, was inhibited by low concentrations of o-vanadate and was insensitive to oxytocin and prostaglandins E2 and F2 alpha. The enzyme activity was maximal at 45 degrees C, pH 7.5-8.0, and at Mg-ATP and Ca2+ concentrations of 1.5-2.5 mM and 5-20 microM, respectively.
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