Abstract
Further purification of highly active tyrosinase inhibitors by DEAE-Sephadex column chromatography revealed that the mode of action of the inhibitors from Greene''s hamster melanomas with different melanogenic status is organelle specific. The inhibitor from amelanotic melanoma has a relatively strong suppressive effect on the tyrosinases in GERL [Golgi, endoplasmic reticulum, lysosome system] and coated vesicle containing fractions. The inhibitor from melanotic melanoma has no substantial effect on these tyrosinases, although melanosomal tyrosinase is inhibited by both. Apparently, the defect of melanization in amelanotic melanoma in vivo is related to the tyrosinase inhibition of the smooth membrane system including GERL and coated vesicle by the highly active inhibitor characteristic of amelanotic melanoma.