Glutathione S-transferases of human brain. Evidence for two immunologically distinct types of 26500-Mr subunits.
Human brain contains one cationic (pI8.3) and two anionic (pI5.5 and 4.6) forms of glutathione S-transferase. The cationic form (pI8.3) and the less-anionic form (pI5.5) do not correspond to any of the glutathione S-transferases previously characterized in human tissues. Both of these forms are dimers of 26500-Mr subunits; however, immunological and catalytic properties indicate that these two enzyme forms are different from each other. The cationic form (pI8.3) cross-reacts with antibodies raised against cationic glutathione S-transferases of human liver, whereas the anionic form (pI5.5) does not. Additionally, only the cationic form expresses glutathione peroxidase activity. The other anionic form (pI4.6) is a dimer of 24500-Mr and 22500-Mr subunits. Two-dimensional gel electrophoresis demonstrates that there are three types of 26500-Mr subunits, two types of 24500-Mr subunits and two types of 22500-Mr subunits present in the glutathione S-transferases of human brain.
D000596:Amino Acids / Q000032:analysis; D001921:Brain / Q000201:enzymology*; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000276:immunology; D006801:Humans; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000276:immunology; D007700:Kinetics; D013379:Substrate Specificity
D000596:Amino Acids; D007527:Isoenzymes; D005982:Glutathione Transferase