Isolation and purification of Ca2+,Mg2+-ATPase from plasma membranes of the myometrium
Slinchenko, N.N.; Liubakovskaia, L.A.; Kurskiĭ, M.D.; Sopel', L.V.
Ukrainskii Biokhimicheskii Zhurnal 62(3): 60-65
1990
ISSN/ISBN: 0201-8470 PMID: 2144381 Document Number: 357158
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.