[Isolation and purification of Ca2+,Mg2+-ATPase from plasma membranes of the myometrium].
The preparation of the purified Ca2+, Mg2(+)-ATPase has been isolated from triton X-100 solubilizate of plasma membranes of the pig myometrium using the method of affinity chromatography on calmodulin-Sepharose 4B. The specific activity of the enzyme shows its 52-fold purification. The enzymic preparation practically has no Mg2(+)-ATPase activity. By the data of DS-Na-electrophoresis in PAAG the Ca2+, Mg2+ ATPase preparation consists of two polypeptides with Mm 130 and 205 kDa. Autoradiography shows their Ca2(+)-dependent phosphorylation. The purified enzyme is highly sensitive to the inhibitory effect of orthovanadate.
Slinchenko
N N
NN
Liubakovskaia
L A
LA
Kurskiĭ
M D
MD
Sopel'
L V
LV
D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000302:isolation & purification*; D000252:Calcium-Transporting ATPases / Q000302:isolation & purification*; D002462:Cell Membrane / Q000201:enzymology; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D009215:Myometrium / Q000201:enzymology*; D012995:Solubility; D013552:Swine
D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases
Vydelenie i ochistka Ca2+,Mg2+-ATP-azy plazmaticheskikh membran miometriia.