Characterization of multiple glutathione transferases from the house fly, Musca domestica (L) |
| |
| Authors: | Alan G Clark NA Shamaan Walter C Dauterman Tatsumi Hayaoka |
| |
| Institution: | 1. Victoria University of Wellington, Private Bag, Wellington, New Zealand;2. Toxicology Program, North Carolina State University, Raleigh, North Carolina 27650 USA |
| |
| Abstract: | Glutathione transferases have been purified to a high degree of homogeneity from three strains of house fly by a procedure involving affinity chromatography on glutathione-sulfobromophthalein conjugate immobilized on Sepharose 4B, followed by preparative isoelectrofocusing. The affinity chromatography yielded purifications of between about 10- and 100-fold, depending on the strain and the substrate with which activity was measured. Each strain was shown to possess several proteins with glutathione S-transferase activity which fell into two clearly defined groups. The first group, of relatively low isoelectric point, showed activity with CDNB but little with DCNB, p-nitrobenzylchloride, or 1,2-epoxy-3-(p-nitrophenoxy)propane, whereas the second group, of higher isoelectric points, showed substantial activity with all substrates tested. Studies on the subunit structure of these enzymes demonstrated the existence of three different sized subunits of Mr 20,000, 22,000, and 23,500. From the experimental evidence recorded here, the existence of at least three functionally different glutathione transferases is inferred. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
