Biochemical characterization of tyrosinase inhibitors using tyrosinase binding affinity chromatography

Purification of tyrosinase inhibitors of hamster melanomas was carried out 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 a 310 molecular weight fraction. They also show characteristics of polypeptides which contain glycine, glutamic acid, serine, proline and alanine as main amino acids.