Source:http://linkedlifedata.com/resource/pubmed/id/16782055
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2006-6-26
|
pubmed:abstractText |
We cloned and sequenced full-length cDNA of a theta-class-like glutathione S-transferase (GST-T) from liver tissue of the self-fertilizing fish Rivulus marmoratus. The full-length cDNA of rm-GST-T was 907 bp in length containing an open reading frame of 666 bp that encoded a 221-amino acid putative protein. Its derived amino acid sequence was clustered with other vertebrate theta-class GSTs in a phylogenetic tree. The deduced amino acid sequence of theta-like rm-GST (rm-GST-T) was compared with both classes (alpha and theta) of GST and alpha-class rm-GST (rm-GST-A). Tissue-specific expression of two rm-GST mRNAs was investigated using real-time RT-PCR. To further characterize the catalytic properties of this enzyme along with rm-GST-A, we constructed the recombinant theta-like rm-GST plasmid with a 6 x His-Tag at the N-terminal of rm-GST-T cDNA. Recombinant rm-GST-T was highly expressed in transformed Escherichia coli, and its soluble fraction was purified by His-Tag affinity column chromatography. The kinetic properties and effects of pH and temperature on rm-GST-T were further studied, along with enzyme activity and inhibition effects, and compared with recombinant rm-GST-A. These results suggest that recombinant rm-GSTs such as rm-GST-A and rm-GST-T play a conserved functional role in R. marmoratus.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
346
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1053-61
|
pubmed:dateRevised |
2010-12-1
|
pubmed:meshHeading |
pubmed-meshheading:16782055-Amino Acid Sequence,
pubmed-meshheading:16782055-Animals,
pubmed-meshheading:16782055-Base Sequence,
pubmed-meshheading:16782055-Cloning, Molecular,
pubmed-meshheading:16782055-Conserved Sequence,
pubmed-meshheading:16782055-Cyprinodontiformes,
pubmed-meshheading:16782055-Enzyme Inhibitors,
pubmed-meshheading:16782055-Glutathione Transferase,
pubmed-meshheading:16782055-Hermaphroditic Organisms,
pubmed-meshheading:16782055-Humans,
pubmed-meshheading:16782055-Isoenzymes,
pubmed-meshheading:16782055-Molecular Sequence Data,
pubmed-meshheading:16782055-Phylogeny,
pubmed-meshheading:16782055-Recombinant Proteins,
pubmed-meshheading:16782055-Sequence Alignment,
pubmed-meshheading:16782055-Sex Determination Processes
|
pubmed:year |
2006
|
pubmed:articleTitle |
Molecular cloning and characterization of theta-class glutathione S-transferase (GST-T) from the hermaphroditic fish Rivulus marmoratus and biochemical comparisons with alpha-class glutathione S-transferase (GST-A).
|
pubmed:affiliation |
Department of Molecular and Environmental Bioscience, and the National Research Laboratory of Marine Molecular and Environmental Bioscience, Graduate School, Hanyang University, Seoul 133-791, South Korea.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|