Localization of a portion of the active site of two rat liver glutathione S-transferases using a photoaffinity label
Open Access
- 1 October 1989
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 264 (30) , 17712-17717
- https://doi.org/10.1016/s0021-9258(19)84629-x
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- Special article the glutathione S-transferases: An updateHepatology, 1989
- Crystallization and a preliminary X-ray diffraction study of isozyme 3-3 of glutathione S-transferase from rat liverJournal of Molecular Biology, 1987
- The basic glutathione S-transferases from human livers are products of separate genesBiochemical and Biophysical Research Communications, 1987
- Human liver glutathione S-transferases: Complete primary sequence of an Ha subunit cDNABiochemical and Biophysical Research Communications, 1986
- Cytosolic rat liver glutathione transferase 4-4. Primary structure of the protein reveals extensive differences between homologous glutathione transferases of classes Alpha and MuEuropean Journal of Biochemistry, 1986
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Photoaffinity labelling by S-(p-azidophenacyl)-glutathione of glyoxalase II and glutathione S-transferaseBiochemical and Biophysical Research Communications, 1980
- A photoaffinity label derivative of glutathione and its inhibition of glyoxalase IFEBS Letters, 1980
- Inhibition of glyoxalase I by S-substituted glutathionesJournal of Medicinal Chemistry, 1971
- Radioimmunoassay of human parathyroid hormone in serumJournal of Clinical Investigation, 1971