Linked Life Data

11668220

Source:http://linkedlifedata.com/resource/pubmed/id/11668220

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2001-10-22
pubmed:abstractText
The recognition of the importance and utility of single nucleotide polymorphisms has generated an interest in the development of new strategies for their identification. Analysis of the Expressed Sequence Tag (EST) database can provide a rapid and efficient means of identifying polymorphisms. Screening of the Alpha class glutathione transferases (GSTs) in the EST database identified 10 putative polymorphisms in the coding region of the GSTA1 and GSTA2 genes, six of which were subsequently verified by sequence analysis. Polymerase chain reaction/restriction fragment length polymorphism analysis revealed the existence of three variants, a silent base substitution, K125K (G365A) in GSTA1, and T112S and E210A in GSTA2, in European Australian, African and Chinese populations. The variant isoforms of GSTA2 were expressed in Escherichia coli, purified, and enzymatically characterized. Modelling of the two GSTA2 polymorphisms into a three-dimensional structure of GSTA2, and characterization of their enzymatic properties, has shown that the structure and function of the wild-type GSTA2-2 isoenzyme is not significantly altered by these polymorphisms. This report demonstrates that analysis of the EST database provides a rapid and efficient means of identifying variant proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0960-314X
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
609-17
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Polymorphism of human Alpha class glutathione transferases.
pubmed:affiliation
Molecular Genetics Group, Division of Molecular Medicine, John Curtin School of Medical Research, Australian National University, Canberra, Australia.
pubmed:publicationType
Journal Article