Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties.

@article{Zimniak1994NaturallyOH,
  title={Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties.},
  author={P. Zimniak and B. Nanduri and S. Pikula and J. Bandorowicz-Pikula and S. Singhal and S. Srivastava and S. Awasthi and Y. Awasthi},
  journal={European journal of biochemistry},
  year={1994},
  volume={224 3},
  pages={
          893-9
        }
}
Glutathione S-transferase P1-1 isoforms, differing in a single amino acid residue (Ile104 or Val104), have been previously identified in human placenta [Ahmad, H., Wilson, D. E., Fritz, R. R., Singh, S. V., Medh, R. D., Nagle, G. T., Awasthi, Y. C. & Kurosky, A. (1990) Arch. Biochem. Biophys. 278, 398-408]. In the present report, the enzymic properties of these two proteins are compared. [I104]glutathione S-transferase P1-1 has been expressed from its cDNA in Escherichia coli and purified to… Expand
Activity of four allelic forms of glutathione S-transferase hGSTP1-1 for diol epoxides of polycyclic aromatic hydrocarbons.
  • X. Hu, H. Xia, +5 authors S. Singh
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
  • 1997
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