Molecular identification of glutathione S-transferase gene and cDNAs of two isotypes from northern quahog (Mercenaria mercenaria).

@article{Feng2009MolecularIO,
  title={Molecular identification of glutathione S-transferase gene and cDNAs of two isotypes from northern quahog (Mercenaria mercenaria).},
  author={Xia Feng and Bal Ram Singh},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2009},
  volume={154 1},
  pages={25-36}
}
Glutathione S-transferases (GSTs) are universally xenobiotic detoxifying enzymes which have been shown to play a unique detoxifying role in northern quahogs. GST consists of two distinct domains: N-terminal domain which contributes residues to form G-site (GSH-binding site) and C-terminal domain which provides residues to form a hydrophobic H-site (second substrate-binding site). In this study, glutathione S-transferases (GSTs) gene and cDNAs of two isotypes from the northern quahog (Mercenaria… CONTINUE READING

Citations

Publications citing this paper.

References

Publications referenced by this paper.
Showing 1-10 of 40 references

Molecular cloning and thermal stress-induced expression of a pi-class glutathione S-transferase (GST) in the Antarctic bivalve Laternula elliptica

M. Kim, Ahn, I.-Y, J. Cheon, H. Park
Comp. Biochem • 2009

Differential responses of biomarkers in tissues of a freshwater mussel, Dreissena polymorpha, to the exposure of sediment extracts with different levels of contamination

A. M. Osman, H. van den Heuvel, P. C. van Noort
J. Appl. Toxicol • 2007
View 2 Excerpts

Marine Glutathione S-Transferases

Marine Biotechnology • 2007
View 10 Excerpts

Biomarkers in fish from dioxin-contaminated fjords.

Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals • 2006
View 2 Excerpts

Similar Papers

Loading similar papers…