title: Characterization of human tyrosinase ectodomain expressed in Escherichia coli.
abstract: The human tyrosinase ectodomain has been expressed in Escherichia coli as a soluble form and purified by immobilized metal affinity column chromatography. The ectodomain exhibited tyrosinase activities toward the hydroxylation and oxidation reactions. Biochemical properties of the ectodomain appeared to be distinct from those of the human tyrosinase, although common features were retained.
authors.affiliation: Laboratory of Biomolecular Chemistry, Department of Chemistry, College of Natural Sciences, Chung-Ang University, Seoul, 156-756, Korea.
authors.forename: Ji-Na
authors.initials: JN
authors.lastname: Kong
authors.forename: Hee-Jin
authors.initials: HJ
authors.lastname: Lee
authors.forename: Dong-Hyun
authors.initials: DH
authors.lastname: Jo
authors.forename: Kwang-Hoon
authors.initials: KH
authors.lastname: Kong
mesh_terms: D055162:Biocatalysis; D004795:Enzyme Stability; D004926:Escherichia coli / Q000378:metabolism*; D006801:Humans; D014442:Monophenol Monooxygenase / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D014442:Monophenol Monooxygenase