Publisher: Bachudo Science Co. Ltd

Substrate Specificity and Inhibition Studies On African Catfish ( CLIRIAS GARIEPINUS)Liver Glutathione S-Transferase

A. O. Kolawole, J. O. Ajele
KEYWORDS: Glutathione transferase; African catfish; Clatias gariepinus; substrate specificity; isoenzyme( s)


The effect of some inhibitors of glutathione transferases was examined on a purified glutathione transferase from the liver of the African catfish (Clarias gariepinus). The ability of the enzyme to catalyze the conjugation of glutathione (GSH) with a variety of other compounds was also examined. The glutathione transferase (GST) from the African catfish was inhibited by all the compounds examined. Cibracron blue and triphenyltin chloride were the most potent inhibitors with 1 50 (concentration of inhibitors causing 50% inhibition) of 0.0875µM and 0.0525µM respectively. The enzyme displayed broad substrate specificity. The enzyme was able to catalyze the conjugation of GSH with 1-chloro-2,4-dinitrobenzene (CDNB), ethacrynic acid , 4-nitrubenzylchloride, p-nitrophenylacetate and hydrogen peroxide. The results obtained from this work suggest that the glutathione transferase from the liver of African catfish might possibly belong to the Pi and Mu class cf isoenzymes and that the enzyme is homodimeric.

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