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Biochemical characterization of tyrosinase inhibitors using tyrosinase binding affinity chromatography
Author(s) -
IMOKAWA GENJI,
MISHIMA YUTAKA
Publication year - 1981
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/j.1365-2133.1981.tb08167.x
Subject(s) - tyrosinase , chemistry , glycine , alanine , serine , biochemistry , affinity chromatography , amino acid , chromatography , enzyme
SUMMARY 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.