Expressed sequence tag analysis for identification and characterization of genes related to Tributyltin (TBT) exposure in the abalone Haliotis diversicolor supertexta

2009 ◽  
Vol 4 (4) ◽  
pp. 255-262 ◽  
Author(s):  
Xiwei Jia ◽  
Ziping Zhang ◽  
Guodong Wang ◽  
Zhihua Zou ◽  
Shuhong Wang ◽  
...  
Keyword(s):  
Expressed Sequence Tag ◽  
Haliotis Diversicolor ◽  
Haliotis Diversicolor Supertexta ◽  
Diversicolor Supertexta ◽  
Expressed Sequence Tag Analysis ◽  
Identification And Characterization ◽  
Expressed Sequence

scholarly journals Expressed Sequence Tag Analysis for Identification and Characterization of Sex-Related Genes in the Giant Tiger Shrimp Penaeus monodon

BMB Reports ◽  
2007 ◽  
Vol 40 (4) ◽  
pp. 501-510 ◽  
Author(s):  
Rachanimuk Preechaphol ◽  
Rungnapa Leelatanawit ◽  
Kanchana Sittikankeaw ◽  
Sirawut Klinbunga ◽  
Bavornlak Khamnamtong ◽  
...  
Keyword(s):  
Expressed Sequence Tag ◽  
Penaeus Monodon ◽  
Tiger Shrimp ◽  
Expressed Sequence Tag Analysis ◽  
Identification And Characterization ◽  
Expressed Sequence

scholarly journals Identification and characterization of GSTT3, a third murine Theta class glutathione transferase

2002 ◽  
Vol 366 (1) ◽  
pp. 323-332 ◽  
Author(s):  
Marjorie COGGAN ◽  
Jack U. FLANAGAN ◽  
Michael W. PARKER ◽  
Vanicha VICHAI ◽  
William R. PEARSON ◽  
...  
Keyword(s):  
Glutathione Transferase ◽  
Expressed Sequence Tag ◽  
Molecular Model ◽  
Binding Pocket ◽  
Gene Encoding ◽  
Hydrophobic Substrate ◽  
Intron Structure ◽  
Identification And Characterization ◽  
Expressed Sequence

A novel Theta class glutathione transferase (GST) isoenzyme from mouse termed mGSTT3 has been identified by analysis of the expressed sequence tag database. The gene encoding mGSTT3 is clustered with the mGSTT1 and mGSTT2 genes on chromosome 10 and has an exon/intron structure that is similar to that of the other Theta class genes. mGSTT3 is expressed strongly in the liver and to a decreasing extent in the kidney and testis. Recombinant mGSTT3-3 expressed in Escherichia coli had a substrate-specificity profile that differed significantly from that of GSTT1-1 and GSTT2-2 isoenzymes. A molecular model of mGSTT3 suggested that, in comparison with GSTT2, a decrease in volume of the hydrophobic substrate-binding site and the loss of the sulphate-binding pocket prevents its use of the GSTT2 substrate 1-menaphthyl sulphate.

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