[Catalytic properties of purified Ca2+,Mg2+-ATPase from the myometrium sarcolemma].
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.
Liubakovskaia
L A
LA
Slinchenko
N N
NN
Burchinskaia
N F
NF
Kurskiĭ
M D
MD
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
D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases
Kataliticheskie svoĭstva ochishchennoĭ Ca2+,Mg2+-ATPazy sarkolemmy miometriia.