Abstract
A novel, α-class glutathione S-transferase (GST) isozyme has been isolated from human liver using glutathione (GSH) affinity chromatography, DEAE-cellulose ion-exchange chromatography, and immunoaffinity chromatography. The isozyme is a dimer of approximately 25,000 M r with blocked N termini. Structural, kinetic, and immunological properties of this enzyme indicate that it belongs to the α class of GSTs. Noticeable differences between the properties of this enzyme and the other α-class GSTs of human liver are its anionic nature (p I 5.0), GSH peroxidase activity toward hydrogen peroxide, and relatively higher GSH conjugating activities toward CDNB and epoxide substrates as compared to other α-class GSTs. Results of these studies indicate that anionic GST ω characterized previously (Y. C. Awasthi, D. D. Dao, and R. P. Saneto, 1980, Biochem. J. 191, 1–10) from human liver is a mixture of GST π and a novel α-class GST. We have, therefore, reassigned the name GST ω to this new α-class anionic GST of human liver.
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