Structural and functional properties of a Ca2+-ATPase from human platelets.
作者： W L Dean , D M Sullivan
DOI: 10.1016/S0021-9258(19)45393-3
关键词:
摘要: An antibody prepared against highly purified rabbit muscle Ca2+-ATPase from sarcoplasmic reticulum has been observed to cross-react with proteins in human platelet membrane vesicles. The specifically precipitated activity solubilized membranes and recognized two polypeptides denatured sodium dodecyl sulfate Mr = 107,000 101,000. Brij 78-solubilized was up 10-fold. preparation consisted mainly of approximately 100,000, 40,000. lower molecular weight protein appeared unrelated activity. vesicles exhibited "negative cooperativity" respect the kinetics ATP hydrolysis. apparent Km for Ca2+ activation ATPase 0.1 microM. Ca2+-dependent phosphorylation by [gamma-32P]ATP at 0 degrees C yielded a maximum 0.2-0.4 nmol PO4/mg that labile pH 7.0 20 C. This result suggests only about 2-4% total is Ca2+-ATPase, which agrees an estimate based on specific (20-50 hydrolyzed/min/mg 30 C). Calmodulin resulted 1.6-fold stimulation even after extensive washing calcium chelator or chlorpromazine. It concluded platelets contain immunochemically related pump enzymatic characteristics are quite similar those ATPase.
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