Linked Life Data

10904869

Source:http://linkedlifedata.com/resource/pubmed/id/10904869

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-11-24
pubmed:abstractText
To carry out biochemical characterizations of human tyrosinase and to provide an unlimited source of the enzyme for further study, an expression plasmid, pHis-Tyrosinase, which contains the entire coding sequence except the signal sequence of a human tyrosinase was constructed and expressed in Escherichia coli. The expressed enzyme was simply purified by an immobilized metal affinity chromatography. The recombinant enzyme had the same electrophoretic mobility as the native enzyme from human melanoma cell and cross-reacted with the polyclonal antibody raised against the native enzyme. The recombinant enzyme retained its catalytic function with both hydroxylating and oxidative activities. Km values for L-tyrosine and L-3,4-dihydroxy-phenylalanine of the recombinant enzyme were 0.17 and 0.36 mM, respectively. The activity of the recombinant enzyme was optimal at pH 7.5. Glutathione notably inhibited the enzymatic activity. This work is a further enzymatic characterization of human tyrosinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1096-4959
pubmed:author
pubmed:issnType
Print
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
563-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Expression and characterization of human tyrosinase from a bacterial expression system.
pubmed:affiliation
Department of Chemistry, College of Natural Science, Chung-Ang University, Seoul, South Korea. khkong@cau.ac.kr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't