Abstract
Tyrosinase was dissolved from the melanosome fraction of Harding-Passey mouse melanoma and purified further by Sephadex G-100 gel filtration and DEAE-cellulose column chromatography. The specific activity of the purified preparation was 763 times as high as that of the original melanosome. Tyrosinase thus isolated showed only a single activity in both the electrophoresis of a polyacrylamide gel and a cellulose acetate. The Km value is the same as those of the original melanosome and the smooth-surfaced-membrane. The relationship between particle bound tyrosinase and solubilized tyrosinase is discussed in this paper.
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