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Glutathione S-transferase AA from rat liver

1976; Elsevier BV; Volume: 175; Issue: 2 Linguagem: Inglês

10.1016/0003-9861(76)90563-4

1096-0384

William H. Habig, M. Pabst, William B. Jakoby,

Genomics, phytochemicals, and oxidative stress

Glutathione S-transferase AA from rat liver was purified to apparent homogeneity as judged by gel filtration and gel electrofocusing. The protein has an isoelectric point near pH 9.9 and a molecular weight of 45,000 and is composed of two apparently identical subunits. The enzyme is most active with 1-chloro-2,4-dinitrobenzene and glutathione as substrates. The catalytic properties of transferase AA are very similar to those of transferase B although the two proteins differ in their ability to bind bilirubin and other ligands, in their amino acid composition, and in their immunological properties. When mixtures of transferase AA with other purified glutathione S-transferases were denatured in 6 m guanidine hydrochloride and then renatured by dilution, no hybrids were formed as judged by gel electrofocusing. Isolation of the enzymes from a single rat liver revealed the presence of each of the known glutathione transferases.