Characterization of Human Tyrosinase Ectodomain Expressed in Escherichia coli (original) (raw)
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.
Keywords: Biochemical properties, Ectodomain, Expression in Escherichia coli, Human tyrosinase
Protein & Peptide Letters
Title: Characterization of Human Tyrosinase Ectodomain Expressed in Escherichia coli
Volume: 17Issue: 8
Author(s): Ji-Na Kong, Hee-Jin Lee, Dong-Hyun Jo and Kwang-Hoon Kong
Affiliation:
Keywords: Biochemical properties, Ectodomain, Expression in Escherichia coli, Human tyrosinase
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 Ji-Na, Lee Hee-Jin, Jo Dong-Hyun and Kong Kwang-Hoon, Characterization of Human Tyrosinase Ectodomain Expressed in Escherichia coli, Protein & Peptide Letters 2010; 17 (8) . https://dx.doi.org/10.2174/092986610791498957
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