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The naturally occurring inhibitor of DOPA autoxidation present in guinea pig skin has been shown to inhibit the oxidation of tyrosine to melanin by both the enzyme tyrosinase and epidermal melanocytes. Two possible modes of action were investigated and the inhibitor was shown to be effective by competing with the enzyme tyrosinase for the substrate. 14 C-labeled tyrosine became irreversibly bound to the inhibitor, thus prevented from further oxidation. Acid hydrolysis of the inhibitor-substrate complex released the tyrosine, which had not been changed.
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Flawn et al. (1970) studied this question.
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