Abstract
Cysteine and a wide range of aromatic carboxylic acids were inhibitors for the activity of a commercially purified mushroom tyrosinase. These compounds exhibited different types of inhibition including competitive, noncompetitive, mixed or uncompetitive. The variations in type and degree of inhibition were dependent upon the nature of the inhibitor and the method used for the determination of enzymatic activity, spectrophotometric or polarographic.
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