title: Isolation of soluble tyrosinase from human melanoma cells.
abstract: In the human melanoma cell tyrosinase exists in a membraneous and a soluble form. The membraneous enzyme has an N-terminal amino acid sequence identical to that predicted from a human c-DNA clone by Kwon et al.. The soluble form has now been isolated by a technique mainly based on the trypsin resistence of the enzyme and the use of hydrophobic interaction chromatography. The specific dopa oxidase activity of the soluble enzyme was 300 mumol/min x mg protein. On isoelectric focusing the enzyme was found in at least ten bands, pI between 3.8-4.6. The molecular weight was found to be 53,000 D. The N-terminal amino acid sequence was the same as that found in the membrane bound form of the enzyme, i.e. the protein maps at the c-albino locus.
authors.affiliation: Department of Pharmacology, University of Lund, Sweden.
authors.forename: A
authors.initials: A
authors.lastname: Wittbjer
authors.forename: G
authors.initials: G
authors.lastname: Odh
authors.forename: A M
authors.initials: AM
authors.lastname: Rosengren
authors.forename: E
authors.initials: E
authors.lastname: Rosengren
authors.forename: H
authors.initials: H
authors.lastname: Rorsman
mesh_terms: D000595:Amino Acid Sequence; D002460:Cell Line; D006801:Humans; D008546:Melanoma, Experimental / Q000473:pathology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D014442:Monophenol Monooxygenase / Q000235:genetics / Q000302:isolation & purification*; D014407:Tumor Cells, Cultured / Q000737:chemistry*
chemical_list: D014442:Monophenol Monooxygenase