Abstract
Summary
Microsomes from bovine aorta contained a magnesium activated or “basic” ATPase activity and a calcium activated ATPase activity that was independent of magnesium. Ca2+ stimulated Mg2+ dependent “extra” ATPase was not demonstrable. Kinetic analyses of the magnesium basic ATPase and calcium ATPase activities suggested that the magnesium activation and calcium activation of ATP hydrolysis probably represent a single enzyme moiety. The ATPase has equal affinity for magnesium and calcium and does not distinguish between them.
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