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ABSTRACT 4‐hexylresorcinol (4HR) was a potent inhibitor of mushroom tyrosinase in crude extracts, causing 90% loss of activity at 100 μM. The concentration of 4HR needed to cause 50% inhibition (I 50 ) was = 5 μM. Partially purified tyrosinase was inhibited by lower concentrations of 4HR and was characterized with an I 50 of = 1 μM. Electro‐phoretic analysis, coupled with isoenzyme staining in the presence and absence of 4HR, showed inhibition of tyrosinase isoforms but not of laccase isoforms.
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Dawley et al. (1993) studied this question.
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