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Title: [Isolation and purification of Ca2+,Mg2+-ATPase from plasma membranes of the myometrium]. Author: Slinchenko NN, Liubakovskaia LA, Kurskiĭ MD, Sopel' LV. Journal: Ukr Biokhim Zh (1978); 1990; 62(3):60-5. PubMed ID: 2144381. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]