The Role of Disulphide Bonds in Heinz Body Attachment to Membranes

Abstract

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.

The distribution and aggregatability of intramembrane particles in phenylhydrazine-treated human erythrocytes

“…between the Heinz-bodies and all of the overlying Band 3 molecules. This is consistent with previously published data [5,21]. The reduction of Acridine orange-induced particle aggregation over numerous Heinz-bodies may reflect a true decrease in the local lateral mobility of the integral membrane proteins due to protein-protein (haemichrome-Band 3) interaction.…”