Studies on Mercapturic Acids
- 1 August 1966
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 60 (2) , 133-139
- https://doi.org/10.1093/oxfordjournals.jbchem.a128411
Abstract
S-Benzylglutathione (BzSG) and some other glutathione derivatives were converted into cysteine derivatives by rat kidney microsomes and served as competitive inhibitors to glutathionase. These conversions were similar to the metabolic breakdown of glutathione by the glutathionase system. Glutathionase was solubilized by treatment with deoxycholate or with heat-treated snake venom; the activity to break down glutathione derivatives was solubilized in parallel with the glutathionase activity. Evidence was presented that the breakdown of glutathione derivatives was catalyzed by the glutathionase of rat kidney microsomes; this suggests that glutathionase participates in the formation of mercapturic acid in animals.This publication has 10 references indexed in Scilit:
- Studies on Mercapturic Acids*Effect of Some Aromatic Compounds on the Level of Glutathione and the Activity of Glutathionase** in the RatThe Journal of Biochemistry, 1966
- RAT-KIDNEY LYSOSOMES: ISOLATION AND PROPERTIESBiochemical Journal, 1965
- AN ENZYME CATALYSING THE CONJUGATION OF EPOXIDES WITH GLUTATHIONEBiochemical Journal, 1965
- An enzyme from rat liver catalysing conjugations with glutathioneBiochemical Journal, 1961
- Metabolism of polycyclic compounds. 15. The conversion of naphthalene into a derivative of glutathione by rat-liver slicesBiochemical Journal, 1960
- The formation of mercapturic acids. 1. Formation of mercapturic acid and the levels of glutathione in tissuesBiochemical Journal, 1959
- The formation of mercapturic acids. 2. The possible role of glutathionaseBiochemical Journal, 1959
- Biochemical studies of toxic agents. 11. The occurrence of premercapturic acidsBiochemical Journal, 1958
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934