Erythrocyte membrane protein damage by oxidation products of phenylhydrazine.

Freshly prepared phenylhydrazine solution in buffer generated oxygen free-radicals and induced lipid peroxidation and aggregations of proteins when incubated with erythrocyte ghosts. The aggregation of protein was inhibitible by superoxide dismutase but not by catalase. When phenylhydrazine was allowed to autoxidize in buffer for several hours and subsequently added to a suspension of erythrocyte membrane, extensive aggregation of protein was still apparent although the membrane lipid peroxidation or generation of .OH radicals was insignificant under such condition. These results implicated oxidation products of phenylhydrazine but not oxygen free-radicals or lipid peroxidation products as major contributors to phenylhydrazine induced protein damages in red blood cells ghosts.