| First Author | Zimniak P | Year | 1994 |
| Journal | J Biol Chem | Volume | 269 |
| Issue | 2 | Pages | 992-1000 |
| PubMed ID | 7904605 | Mgi Jnum | J:16442 |
| Mgi Id | MGI:64523 | Doi | 10.1016/s0021-9258(17)42210-1 |
| Citation | Zimniak P, et al. (1994) Estimation of genomic complexity, heterologous expression, and enzymatic characterization of mouse glutathione S-transferase mGSTA4-4 (GST 5.7). J Biol Chem 269(2):992-1000 |
| abstractText | We have previously isolated a cDNA clone for a unique mouse lung glutathione S-transferase, mGSTA4-4 (GST 5.7) (Zimniak, P., Eckles, M. A., Saxena, M., and Awasthi, Y. C. (1992) FEBS Lett. 313, 173-176). By genomic Southern blotting and polymerase chain reaction single strand conformation polymorphism analysis we have now demonstrated the presence of at least two mGSTA4-related genes in the mouse. The heterogeneity of mGSTA4-4 was further examined by comparing the structural and kinetic properties of mGSTA4-4 isolated from mouse lung with those of recombinant rec-mGSTA4-4 expressed in Escherichia coli. Except for the isoelectric point, the physical properties of the two proteins were indistinguishable. Western blots using antibodies against rec-mGSTA4-4 have shown selective expression of the enzyme in mouse tissues. Even though the substrate specificity profiles of the tissue-isolated and recombinant enzymes, which point to a role of mGSTA4-4 in the detoxification of lipid peroxidation products, were generally similar, significant differences were observed with selected substrates. The existence of functionally distinct forms of mGSTA4-4 and the presence of more than one gene strongly suggest that the previously observed differences in properties of mGSTA4-4 isolated from various mouse tissues (Awasthi, S., Singhal, S. S., Srivastava, S. K., and Awasthi, Y. C. (1993) Arch. Biochem. Biophys. 301, 143-150) may be due to tissue-specific expression of mGSTA4-related genes. |
