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. 1967 Apr;103(1):49–54. doi: 10.1042/bj1030049

Species differences in the inhibition of glutathione S-aryltransferase by phthaleins and dicarboxylic acids

A G Clark 1, F J Darby 1, J N Smith 1
PMCID: PMC1270367  PMID: 6033774

Abstract

1. Glutathione-S-aryltransferase activity from grass grubs (Costelytra zealandica) was inhibited by phthaleins, sulphonphthaleins and some dicarboxylic acids. 2. These compounds had no detectable action on the enzyme from sheep liver. 3. In insect enzyme the inhibition was competitive with respect to glutathione and non-competitive with respect to the aromatic substrate. 4. Michaelis constants and inhibitor constants were measured for sheep-liver or grass-grub enzyme between pH5 and pH10 and evidence was obtained for the presence of two groups with pK9·2 in the glutathione-binding site of the insect enzyme. 5. Only one such group was detected in the sheep-liver enzyme.

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Selected References

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

  1. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BRADBURY F. R., STANDEN H. Metabolism of benzene hexachloride by resistant houseflies Musca domestica. Nature. 1959 Apr 4;183(4666):983–984. doi: 10.1038/183983b0. [DOI] [PubMed] [Google Scholar]
  3. Booth J., Boyland E., Sims P. An enzyme from rat liver catalysing conjugations with glutathione. Biochem J. 1961 Jun;79(3):516–524. doi: 10.1042/bj0790516. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Clark A. G., Hitchcock M., Smith J. N. Metabolism of gammexane in flies, ticks and locusts. Nature. 1966 Jan 1;209(5018):103–103. doi: 10.1038/209103a0. [DOI] [PubMed] [Google Scholar]
  6. Cohen A. J., Smith J. N., Turbert H. Comparative detoxication. 10. The enzymic conjugation of chloro compounds with glutathione in locusts and other insects. Biochem J. 1964 Mar;90(3):457–464. doi: 10.1042/bj0900457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DIXON M. The effect of pH on the affinities of enzymes for substrates and inhibitors. Biochem J. 1953 Aug;55(1):161–170. doi: 10.1042/bj0550161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. DIXON M. The effect of pH on the affinities of enzymes for substrates and inhibitors. Biochem J. 1953 Aug;55(1):161–170. doi: 10.1042/bj0550161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. FLORINI J. R., VESTLING C. S. Graphical determination of the dissociation constants for two-substrate enzyme systems. Biochim Biophys Acta. 1957 Sep;25(3):575–578. doi: 10.1016/0006-3002(57)90529-2. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Grover P. L., Sims P. The metabolism of gamma-2,3,4,5,6-pentachlorocyclohex-1-ene and gamma-hexachlorocyclohexane in rats. Biochem J. 1965 Aug;96(2):521–525. doi: 10.1042/bj0960521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. ISHERWOOD F. A. Chemistry and biochemistry of glutathione. Biochem Soc Symp. 1959;17:3–16. [PubMed] [Google Scholar]

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