Evidence for two forms of ligandin (YaYa dimers of glutathione S-transferase) in rat liver and kidney.
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.
D000818:Animals; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000302:isolation & purification; D007527:Isoenzymes / Q000302:isolation & purification; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats
D007527:Isoenzymes; D010446:Peptide Fragments; D005982:Glutathione Transferase