Effect of the diazonium salt of sulfanilic acid on human erythrocyte ATPase activity |
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Authors: | Stanley J Masiak Guy DAngelo |
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Institution: | Dept. of Physiology and Biophysics, Health Sciences Center, State University of New York, Stony Brook, New York 11790 U.S.A. |
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Abstract: | External treatment of human erythrocytes with the diazonium salt of sulfanilic acid does not inhibit the Mg2+-dependent ATPase but does markedly inhibit the Ca2+-stimulated ATPase activity. Inhibition of the (Na+ + K+)-dependent activity is dependent upon the concentration of diazonium salt used. Treatment of membrane fragments does not irreversibly inhibit the (Na+ + K+)-dependent ATPase even though the diazonium salt binds covalently to membrane components. However, the Mg2+-dependent and Ca2+-stimulated ATPase activities are irreversibly inhibited. ATP and Mg-ATP will completely protect the (Na+ + K+)-dependent ATPase when present during treatment of membrane fragments with the diazonium salt, but only Mg-ATP will protect the Mg2+-dependent ATPase from inhibition. The Ca2+-stimulated ATPase activity is not protected. |
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