| First Author | Mainwaring GW | Year | 1996 |
| Journal | Biochem J | Volume | 314 ( Pt 2) |
| Pages | 445-8 | PubMed ID | 8670055 |
| Mgi Jnum | J:32863 | Mgi Id | MGI:80351 |
| Doi | 10.1042/bj3140445 | Citation | Mainwaring GW, et al. (1996) Isolation of a mouse theta glutathione S-transferase active with methylene chloride. Biochem J 314(Pt 2):445-8 |
| abstractText | A glutathione S-transferase metabolizing methylene chloride has been isolated from mouse liver using a variety of chromatographic methods. N-terminal and internal amino acid sequences show that the enzyme, designated GST T1-1*, is closely related to the rat Theta-class GST 5-5. The mouse enzyme, molecular mass 25000 Da, has been isolated to homogeneity in active form with an approximate yield of 2% of the cytosolic activity towards methylene chloride. GST T1-1* has a specific activity of about 5.5 micromol/min per mg of protein whereas the rat GST 5-5 is reported to have a specific activity of about 11 micromol/min per mg of protein [Meyer, Coles, Pemble, Gilmore, Fraser and Ketterer (1991) Biochem. J. 274, 409-414], demonstrating that both the rat and mouse enzymes have similar activity with this substrate. Limited evidence was obtained for a second enzyme, with a similar molecular mass (25400 Da), which had an N-terminal sequence identical to that of rat GST 12-12. This protein, which was sequenced from a band on a gel, was extremely labile and could not be isolated to homogeneity. The partially purified enzyme was not active with methylene chloride. |
