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- W2073248857 abstract "This report presents studies on the effect of diamide on protein phosphorylation in erythrocyte membranes. Diamide, a thiol-oxidizing reagent, nonspecifically inhibits cyclic AMP-dependent and -independent autophosphorylation of red cell membranes, but not the activity of the solubilized membrane cyclic AMP-independent protein kinases. Analysis of diamide-treated membranes by gel electrophoresis indicates that diamide is capable of inducing cross-linking of membrane proteins. The action of diamide, both in the inhibition of membrane autophosphorylation and in the cross-linking of membrane proteins, is very similar to that of Cu2+ · o-phenanthroline complex. Our data indicate that diamide inhibits erythrocyte membrane autophosphorylation by perturbing the protein substrates." @default.
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- W2073248857 title "Inhibition of protein phosphorylation and induction of protein cross-linking in erythrocyte membranes by diamide" @default.
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- W2073248857 doi "https://doi.org/10.1016/0005-2736(78)90392-9" @default.
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