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Solubilization and Activation of Mammalian Melanoma Particulate Tyrosinase by Lipase Digestion¹

Department of Biology, Wayne State University, Detroit, Michigan 48202, and Michigan Cancer Foundation, Detroit, Michigan 48201

Digestion of mammalian melanoma particulate tyrosinase with lipase resulted in 261 to 3,000% solubilization and 900 to 7,000% activation of the enzyme. The solubilization of the enzyme was verified by assay of melanin-¹⁴C in the 144,000 x g supernatant of the lipase-digested mixture, and the activation was evaluated by comparison of the activities obtained before and after lipase digestion. The highest activity obtained in the 144,000 x g supernatant of the lipase-digested mixture expressed as percentage of the original activity in the particulate fraction was 261% for human melanoma and 3,000% for B-16 mouse melanoma. The highest activation of the particulate tyrosinase by lipase digestion was 900% for human melanoma and 7,000% for mouse melanoma.

¹ This investigation was supported by USPHS Research Grants CA-12731-02 and CA-15991-01 from the National Cancer Institute. Contribution No. 321, Department of Biology, Wayne State University.

Received 3/25/74. Accepted 8/22/74.