The role of disulphide bonds in Heinz body attachment to membranes.
The mechanism of binding of oxidant-induced Heinz bodies to red cell membrane was studied. Heinz bodies induced by acetylphenylhydrazine in intact cells or in the presence of membrane remained attached to membrane when separated by a sucrose gradient. Incubation with sulphydryl reagents failed to free intact Heinz bodies from or prevent attachment to membranes, although the amount of haem was reduced. Thus disulphide bonds do not appear to be a major mechanism of attachment of Heinz bodies to red cell membrane.
D001665:Binding Sites; D002458:Cell Fractionation; D002462:Cell Membrane / Q000378:metabolism; D004220:Disulfides / Q000097:blood*; D004229:Dithiothreitol / Q000494:pharmacology; D004912:Erythrocytes / Q000378:metabolism*; D006366:Heinz Bodies / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D006801:Humans; D008623:Mercaptoethanol / Q000494:pharmacology; D014508:Urea / Q000494:pharmacology
D004220:Disulfides; D006418:Heme; D008623:Mercaptoethanol; D014508:Urea; D004229:Dithiothreitol