Purification of a water-soluble Mg2+-ATPase from human erythrocyte membranes |
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Authors: | MD White GB Ralston |
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Institution: | Department of Biochemistry, University of Sydney, Sydney, N.S.W. 2006 Australia |
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Abstract: | A water-soluble Mg2+-ATPase previously reported (White, M.D. and Ralston, G.B. (1976) Biochim. Biophys. Acta 436, 567–576) has been purified from human erythrocyte membranes. The purified enzyme has a molecular weight of 575 000; the apparent minimum molecular weight was 100 000, corresponding to a soluble protein of the component 3 region. The value for ATP was 1 mM and apparent for Mg2+ was 3.6 mM. By means of histochemical activity staining in acrylamide gels it was shown that the purified ATPase preparation could be inhibited by Cd2+ and Zn2+ salts, and , known inhibitors of membrane endocytosis. |
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Keywords: | Membrane protein Endocytosis (Erythrocyte membrane) |
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