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Characterization of Human Tyrosinase Ectodomain Expressed in Escherichia coli

Authors
Kong, Ji-NaLee, Hee-JinJo, Dong-HyunKong, Kwang-Hoon
Issue Date
2010
Publisher
BENTHAM SCIENCE PUBL LTD
Keywords
Biochemical properties; Ectodomain; Expression in Escherichia coli; Human tyrosinase
Citation
PROTEIN AND PEPTIDE LETTERS, v.17, no.8, pp 1026 - 1030
Pages
5
Journal Title
PROTEIN AND PEPTIDE LETTERS
Volume
17
Number
8
Start Page
1026
End Page
1030
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/22788
DOI
10.2174/092986610791498957
ISSN
0929-8665
1875-5305
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.
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Kong, Kwang-Hoon
자연과학대학 (화학과)
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