Isoelectric focusing of brain cortex GSH S-transferase activity in mammals: evidence that polymorphism is absent in man.
Specific activities of GSH S-transferase toward different model substrates were determined in the cytosol prepared from rat, guinea pig, rabbit, mouse, sheep, beef, pig and human brain cortex. The GSH S-transferase composition of the eight mammalian brain cortices was studied by using density gradient isoelectric focusing technique. Human brain cortex GSH S-transferase was resolved into a single peak of activity centered at pH 4.6, whereas the supernatants of all other mammals consisted of more than one enzymatic form. The kinetic properties of all forms isolated were compared.
D000328:Adult; D000818:Animals; D001932:Brain Neoplasms / Q000201:enzymology; D002540:Cerebral Cortex / Q000201:enzymology*; D003600:Cytosol / Q000201:enzymology; D005982:Glutathione Transferase / Q000235:genetics / Q000302:isolation & purification*; D006168:Guinea Pigs; D006801:Humans; D051379:Mice; D011110:Polymorphism, Genetic; D011817:Rabbits; D051381:Rats; D012756:Sheep; D013045:Species Specificity; D013552:Swine
D005982:Glutathione Transferase