Inhibition of protein phosphorylation and induction of protein cross-linking in erythrocyte membranes by diamide.
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 memvranes, but not the activity of the solubilized membrane cycle 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.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001391:Azo Compounds / Q000494:pharmacology*; D003958:Diamide / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000097:blood*; D010618:Phenanthrolines / Q000494:pharmacology; D010750:Phosphoproteins / Q000097:blood; D011494:Protein Kinases / Q000378:metabolism; D011817:Rabbits; D013045:Species Specificity
D001391:Azo Compounds; D008565:Membrane Proteins; D010618:Phenanthrolines; D010750:Phosphoproteins; D003958:Diamide; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D011494:Protein Kinases