Biochemical characterization of tyrosinase inhibitors using tyrosinase binding affinity chromatography

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Abstract
Tyrosinase inhibitors of hamster melanomas were purified using tyrosinase binding affinity column chromatography. This method enables the isolation of tyrosinase inhibitors with a 124-fold purification index as compared to that of crude preparation after dialysation. The purified inhibitors consist of a mixture of 5000-6000 and 310 MW fraction. They show characteristics of polypeptides which contain glycine, glutamic acid, serine, proline and alanine as main amino acids.