Phenylhydrazine causes sulfhydryl oxidation and protein aggregation in hemoglobin-free human erythrocyte membranes.

Phenylhydrazine induces a remarkable decrease in total free sulfhydryls as well as spectrin and most other polypeptides in hemoglobin-free human erythrocyte ghosts. A parallel increase in coomassie blue stainable material that was retained on the gel tops was also observed. EDTA but not DM protected the membrane from phenylhydrazine-induced alterations, while antioxidants, catalase and SOD were ineffective. The aggregated material isolated from phenylhydrazine-treated membranes could be partially dissociated in presence of beta-mercaptoethanol to yield most of the membrane polypeptides.