Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1967 Jul;104(1):95–102. doi: 10.1042/bj1040095

Enzyme-catalysed conjugations of glutathione with unsaturated compounds

E Boyland 1, L F Chasseaud 1
PMCID: PMC1270549  PMID: 6035529

Abstract

1. Rat-liver supernatant catalyses the reaction of diethyl maleate with glutathione. 2. Evidence is presented that the enzyme involved is different from the known glutathione-conjugating enzymes, glutathione S-alkyltransferase, S-aryltransferase and S-epoxidetransferase. 3. Rat-liver supernatant catalyses the reaction of a number of other αβ-unsaturated compounds, including aldehydes, ketones, lactones, nitriles and nitro compounds, with glutathione: separate enzymes may be responsible for these reactions.

Full text

PDF
95

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AL-KASSAB S., BOYLAND E., WILLIAMS K. An enzyme from rat liver catalysing conjugations with glutathione. 2. Replacement of nitro groups. Biochem J. 1963 Apr;87:4–9. doi: 10.1042/bj0870004. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ANGIELSKI S., ROGULSKI J. [Effect of kidney homogenates on the reaction of glutathione with maleic acid]. Acta Biochim Pol. 1961;8:89–103. [PubMed] [Google Scholar]
  3. BARNES M. M., JAMES S. P., WOOD P. B. The formation of mercapturic acids. 1. Formation of mercapturic acid and the levels of glutathione in tissues. Biochem J. 1959 Apr;71(4):680–690. doi: 10.1042/bj0710680. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BOYLAND E., WILLIAMS K. AN ENZYME CATALYSING THE CONJUGATION OF EPOXIDES WITH GLUTATHIONE. Biochem J. 1965 Jan;94:190–197. doi: 10.1042/bj0940190. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. BRAY H. G., FRANKLIN T. J., JAMES S. P. The formation of mercapturic acids. 2. The possible role of glutathionase. Biochem J. 1959 Apr;71(4):690–696. doi: 10.1042/bj0710690. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Baer J. E., Beyer K. H. Renal pharmacology. Annu Rev Pharmacol. 1966;6:261–292. doi: 10.1146/annurev.pa.06.040166.001401. [DOI] [PubMed] [Google Scholar]
  7. CALAM D. H., WALEY S. G. Acidic peptides of the lens. 8. S-(alpha beta-dicarboxyethyl) glutathione. Biochem J. 1963 Feb;86:226–231. doi: 10.1042/bj0860226. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. COMBES B., STAKELUM G. S. A liver enzyme that conjugates sulfobromophthalein sodium with glutathione. J Clin Invest. 1961 Jun;40:981–988. doi: 10.1172/JCI104337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. DICKENS F. CARCINOGENIC LACTONES AND RELATED SUBSTANCES. Br Med Bull. 1964 May;20:96–101. doi: 10.1093/oxfordjournals.bmb.a070324. [DOI] [PubMed] [Google Scholar]
  10. Deichmann W. B., Mac Donald W. E., Lampe K. F., Dressler I., Anderson W. A. Nitro-oolefins as potential carcinogens in air pollution. Ind Med Surg. 1965 Oct;34(10):800–807. [PubMed] [Google Scholar]
  11. ELLMAN G. L. Tissue sulfhydryl groups. Arch Biochem Biophys. 1959 May;82(1):70–77. doi: 10.1016/0003-9861(59)90090-6. [DOI] [PubMed] [Google Scholar]
  12. Grover P. L., Sims P. Conjugations with glutathione. Distribution of glutathione S-aryltransferase in vertebrate species. Biochem J. 1964 Mar;90(3):603–606. doi: 10.1042/bj0900603. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Johnson M. K. Studies on glutathione S-alkyltransferase of the rat. Biochem J. 1966 Jan;98(1):44–56. doi: 10.1042/bj0980044. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Johnson M. K. The influence of some aliphatic compounds on rat liver glutathione levels. Biochem Pharmacol. 1965 Sep;14(9):1383–1385. doi: 10.1016/0006-2952(65)90122-x. [DOI] [PubMed] [Google Scholar]
  15. Kuwaki T., Mizuhara S. S-(1-2-dicarboxyethyl)cysteine in urine and kidney. Biochim Biophys Acta. 1966 Feb 28;115(2):491–493. doi: 10.1016/0304-4165(66)90449-1. [DOI] [PubMed] [Google Scholar]
  16. TREON J. F., SIGMON H. The toxicity of methyl and ethyl acrylate. J Ind Hyg Toxicol. 1949 Nov;31(6):317–326. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES