Oxidation of human serum albumin by polyphenol oxidase

Polyphenol oxidase (PPO) oxidizes, due to their tyrosine content, the proteins histone, casein and human serum albumin. These oxidations are inhibited by ascorbate which lowers the redox potential of the medium. Serum albumin in its native state is only moderately oxidized. If, however, prior to oxidation, the albumin is subjected to denaturation, involving unfolding of the chain, the attack by the enzyme is markedly increased. Such denaturation was effected by either the action of dodecyl sulfate or heating to 60°C. The implications of these findings to the problem of senescence are discussed.