Characterization of human tyrosinase ectodomain expressed in Escherichia coli.
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.
Kong
Ji-Na
JN
Laboratory of Biomolecular Chemistry, Department of Chemistry, College of Natural Sciences, Chung-Ang University, Seoul, 156-756, Korea.
Lee
Hee-Jin
HJ
Jo
Dong-Hyun
DH
Kong
Kwang-Hoon
KH
D055162:Biocatalysis; D004795:Enzyme Stability; D004926:Escherichia coli / Q000378:metabolism*; D006801:Humans; D014442:Monophenol Monooxygenase / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D014442:Monophenol Monooxygenase