Characterization of the phosphorylated intermediate of the isolated high-affinity (Ca2+ + Mg2+)-ATPase of human erythrocyte membranes |
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Authors: | Rosemarie Lichtner H. Uwe Wolf |
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Affiliation: | Abteilung Pharmakologie und Toxikologie der Universität Ulm, Oberer Eselsberg N26, D-7900 Ulm/Donau F.R.G. |
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Abstract: | Phosphorylation of solubilized and purified high-affinity (Ca2+ + Mg2+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) of human erythrocyte membranes shows no dependence on cyclic AMP concentration in the range 0.1–1000 μM.Ca2+-dependent phosphoprotein is sensitive to hydroxylamine and molybdate treatment. The phosphate linkage shows maximum stability at low pH values, which is progressively lost as the pH rises, with a shoulder around pH 6. SDS gel electrophoresis of the phosphorylated protein yields a peak which shows relative mobility corresponding to a molecular weight of 145 000 and sensitivity to MgATP-chase and hydroxylamine treatment. This indicates that the phosphoprotein represents the phosphorylated intermediate of the high-affinity (Ca2+ + Mg2+)-ATPase of human erythrocyte membranes. |
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Keywords: | Acylphosphate bond Phosphoprotein (Erythrocyte membrane) |
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