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. 1984 Mar 15;218(3):893–897. doi: 10.1042/bj2180893

Evidence for two forms of ligandin (YaYa dimers of glutathione S-transferase) in rat liver and kidney.

D Sheehan, T J Mantle
PMCID: PMC1153420  PMID: 6721840

Abstract

CM-cellulose chromatography of rat liver and kidney cytosol at pH6 reveals the presence of a second Ya-subunit dimer of glutathione S-transferase (GST-F) in addition to the recently described GST-YaYa (GST-L; our nomenclature) [Hayes & Clarkson (1982) Biochem. J. 207, 459-470]. The two forms are structurally similar (by the criteria of CNBr- and Staphylococcus-V8-proteinase-cleavage peptide maps), and both are sensitive to inhibition by haemin. However, their kinetic parameters with 1-chloro-2,4-dinitrobenzene are quite distinct, and they show differential inducibility by phenobarbitone. These results suggest a similar heterogeneity in Ya-subunits to that previously described for Yb-subunits of glutathione S-transferase and indicate that significant gene duplication may have occurred in these multifunctional intracellular binding proteins.

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Selected References

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

  1. Daniel V., Sarid S., Bar-Nun S., Litwack G. Rat ligandin mRNA molecular cloning and sequencing. Arch Biochem Biophys. 1983 Nov;227(1):266–271. doi: 10.1016/0003-9861(83)90370-3. [DOI] [PubMed] [Google Scholar]
  2. Habig W. H., Pabst M. J., Fleischner G., Gatmaitan Z., Arias I. M., Jakoby W. B. The identity of glutathione S-transferase B with ligandin, a major binding protein of liver. Proc Natl Acad Sci U S A. 1974 Oct;71(10):3879–3882. doi: 10.1073/pnas.71.10.3879. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Habig W. H., Pabst M. J., Jakoby W. B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem. 1974 Nov 25;249(22):7130–7139. [PubMed] [Google Scholar]
  4. Hayes J. D., Clarkson G. H. Purification and characterization of three forms of glutathione S-transferase A. A comparative study of the major YaYa-, YbYb- and YcYc-containing glutathione S-transferases. Biochem J. 1982 Dec 1;207(3):459–470. doi: 10.1042/bj2070459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hayes J. D. Rat liver glutathione S-transferases. A study of the structure of the basic YbYb-containing enzymes. Biochem J. 1983 Sep 1;213(3):625–633. doi: 10.1042/bj2130625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hayes J. D., Strange R. C., Percy-Robb I. W. Cholic acid binding by glutathione S-transferases from rat liver cytosol. Biochem J. 1980 Jan 1;185(1):83–87. doi: 10.1042/bj1850083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hayes J. D., Strange R. C., Percy-Robb I. W. Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S-transferase B. Biochem J. 1979 Sep 1;181(3):699–708. doi: 10.1042/bj1810699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jakoby W. B. The glutathione S-transferases: a group of multifunctional detoxification proteins. Adv Enzymol Relat Areas Mol Biol. 1978;46:383–414. doi: 10.1002/9780470122914.ch6. [DOI] [PubMed] [Google Scholar]
  9. Kalinyak J. E., Taylor J. M. Rat glutathione S-transferase. Cloning of double-stranded cDNA and induction of its mRNA. J Biol Chem. 1982 Jan 10;257(1):523–530. [PubMed] [Google Scholar]
  10. Mannervik B., Guthenberg C. Glutathione transferase (human placenta). Methods Enzymol. 1981;77:231–235. doi: 10.1016/s0076-6879(81)77030-7. [DOI] [PubMed] [Google Scholar]
  11. Mannervik B., Jensson H. Binary combinations of four protein subunits with different catalytic specificities explain the relationship between six basic glutathione S-transferases in rat liver cytosol. J Biol Chem. 1982 Sep 10;257(17):9909–9912. [PubMed] [Google Scholar]
  12. Scully N. C., Mantle T. J. Studies on the nature of the multiple forms of the glutathione S-transferases. Biochem Soc Trans. 1980 Aug;8(4):451–452. doi: 10.1042/bst0080451. [DOI] [PubMed] [Google Scholar]
  13. Scully N. C., Mantle T. J. Tissue distribution and subunit structures of the multiple forms of glutathione S-transferase in the rat. Biochem J. 1981 Jan 1;193(1):367–370. doi: 10.1042/bj1930367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Tu C. P., Weiss M. J., Karakawa W. W., Reddy C. C. Cloning and sequence analysis of a cDNA plasmid for one of the rat liver glutathione S-transferase subunits. Nucleic Acids Res. 1982 Sep 25;10(18):5407–5419. doi: 10.1093/nar/10.18.5407. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Tu C. P., Weiss M. J., Reddy C. C. Subunit composition of rat liver glutathione S-transferases. Biochem Biophys Res Commun. 1982 Sep 30;108(2):461–467. doi: 10.1016/0006-291x(82)90851-8. [DOI] [PubMed] [Google Scholar]
  16. Yalçin S., Jensson H., Mannervik B. A set of inhibitors for discrimination between the basic isozymes of glutathione transferase in rat liver. Biochem Biophys Res Commun. 1983 Jul 29;114(2):829–834. doi: 10.1016/0006-291x(83)90856-2. [DOI] [PubMed] [Google Scholar]

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