Studies on the developmental expression of glutathione S-transferase isoenzymes in human heart and diaphragm.
The developmental expression of the basic, near-neutral and acidic isoenzymes of glutathione S-transferase (RX:glutathione R-transferase, EC 2.5.1.18) has been studied in heart and diaphragm. Neither these enzymes nor the putative muscle-specific GST4 isoenzyme demonstrated any developmental trends in expression. In vitro hybridisation and SDS-discontinuous polyacrylamide gel electrophoresis were used to show that the GST4 isoenzyme is a homodimer composed of monomers that have a slightly larger molecular weight than the near-neutral isoenzyme. The sensitivity of GST4 to inhibitors also appeared similar to that of the GST1 2 isoenzyme. Immunodiffusion and immunoblotting techniques were used to show that the acidic enzyme in muscle is immunologically identical to that in other tissues.
D002845:Chromatography; D003600:Cytosol / Q000201:enzymology; D003964:Diaphragm / Q000196:embryology / Q000201:enzymology / Q000254:growth & development*; D004591:Electrophoresis, Polyacrylamide Gel; D005333:Fetus / Q000201:enzymology*; D005865:Gestational Age; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006321:Heart / Q000196:embryology / Q000254:growth & development*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007118:Immunoassay; D005779:Immunodiffusion; D007223:Infant; D007231:Infant, Newborn; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000378:metabolism*; D024510:Muscle Development; D009206:Myocardium / Q000201:enzymology*
D007527:Isoenzymes; D005982:Glutathione Transferase