Reactive sulfhydryl and disulfide groups of protyrosinase and tyrosinase.

Abstract

Summary and ConclusionsIt seems evident that no change in sulfhydryl nor disulfide groups occurs upon activation of protyrosinase and further that the sulfhydryl and disulfide groups do not seems essential for enzyme activity. Any apparent inhibition caused by oxidation of the sulfhydryl groups or the reduction of the disulfide groups is due to a reaction of the oxidant or reductant with the intermediary products of the oxidation of tyramine-HCL. If the production of tyrosinase is occasioned by the denaturation of an inhibitor, an increase in-SH groups seems probable; this, however, is not the case.