Isoelectric focusing of glutathione S-transferases: Comparison of the acidic transferases from human liver, kidney, lung, spleen and placenta
- 1 January 1983
- journal article
- research article
- Published by Taylor & Francis in Scandinavian Journal of Clinical and Laboratory Investigation
- Vol. 43 (2), 133-139
- https://doi.org/10.1080/00365518309168235
Abstract
The glutathion S-transferase composition of human liver, kidney, lung, spleen and placenta was studied by density gradient isoelectric focusing. On the basis of the enzyme distribution, it was possible to divide the supernatants into 2 groups: one having a predominance of basic activity, the other acidic. Each supernatant consisted of > 1 transferase. Human liver and kidney, 2 major detoxifying organs in the body, bore a clear predominance of basic enzymes, and they had the highest transferase activities. The activity of the other organs consisted of almost only a single acidic transferase. Properties of the major acidic transferases from the organs were compared. Prior to the studies, the enzymes underwent partial 2-step purification. According to the comparison, it seems evident that the major acidic transferases from human kidney, lung, spleen and placenta are either closely related or identical.This publication has 14 references indexed in Scilit:
- Glutathione S-Transferase Activity in Human Fetal and Adult TissuesPharmacology, 1981
- Glutathione S-transferases in earthworms (Lumbricidae). Substrate specificity, tissue and species distribution and molecular weightComparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1981
- Purification of a new glutathione S-transferase (transferase μ) from human liver having high activity with benzo(α)pyrene-4,5-oxideBiochemical and Biophysical Research Communications, 1981
- Interrelationship between anionic and cationic forms of glutathione S-transferases of human liverBiochemical Journal, 1980
- Glutathione S-transferase activity in human placentaBiochemical Pharmacology, 1980
- Inhibition of microsome-mediated binding of aflatoxin B1 to DNA by glutathione S-transferaseCancer Letters, 1980
- Acid glutathione S-transferase from human liver: preliminary reportScandinavian Journal of Clinical and Laboratory Investigation, 1980
- Glutathione transferase from human erythrocytesArchives of Biochemistry and Biophysics, 1978
- The purification by affinity chromatography of a glutathione S-transferase from larvae ofLife Sciences, 1977
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951