title: [Catalytic properties of purified Ca2+,Mg2+-ATPase from the myometrium sarcolemma].
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.
authors: L A
authors: LA
authors: Liubakovskaia
authors: N N
authors: NN
authors: Slinchenko
authors: N F
authors: NF
authors: Burchinskaia
authors: M D
authors: MD
authors: Kurskiĭ
mesh_terms: D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000737:chemistry* / Q000302:isolation & purification; D000252:Calcium-Transporting ATPases / Q000737:chemistry* / Q000302:isolation & purification; D002384:Catalysis; D002846:Chromatography, Affinity; D005260:Female; D006863:Hydrogen-Ion Concentration; D009215:Myometrium / Q000201:enzymology*; D012508:Sarcolemma / Q000201:enzymology*; D013552:Swine
chemical_list: D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases
vernacular_title: Kataliticheskie svoĭstva ochishchennoĭ Ca2+,Mg2+-ATPazy sarkolemmy miometriia.