Phenylhydrazine mediated degradation of bovine serum albumin and membrane proteins of human erythrocytes.

Phenylhydrazine in solution has been shown to produce hydroxyl radicals, as measured by 2-deoxyribose degradation assay. In vitro incubation of bovine serum albumin with phenylhydrazine leads to extensive degradation of the former which, however, is not inhibited by hydroxyl-radical scavengers like mannitol, Tris or n-butanol. Metal chelators like EDTA, however, inhibits the breakdown of BSA. Erythrocyte ghosts incubated in vitro with phenylhydrazine also show extensive loss of membrane cytoskeletal proteins, inhibited by 5 mM EDTA but not by mannitol. In both the occasions a hydroxyl-radical mediated damage to protein takes place by a 'site-specific mechanism'. Further, such a damage to erythrocyte membrane proteins by phenylhydrazine may be related to well known action of this compound in producing accelerated aging of erythrocytes.