Hepatic Cytosolic Glutathione S-Transferases Of Ostrich (Struthio Camelus): Partial Characterization And Interaction With Xenobiotics

The glutathione S-transferases (GSTs) in affinity purified pools of male and female ostrich liver were studied. The GSTs were purified from crude liver cytosols by S-hexylglutathione sepharose affinity chromatography with yields comparable to those reported for GST from mammalian livers. The K, for both glutathione (GSH) and 1-chloro-2,4-dinitroSenzenzene (CDNB) were determined and found to be within the range of values known for mammalian and invertebrate species. 1- chloro-2,4-dinitrobenzene proved to be the best of nine substrates tested to measure activity. Activity was inhibited by bromosulphophthalein and cibacron blue which are well known inhibitors of the mammalian enzyme. Our results indicate that the ostrich liver enzymes behave similarly to the mammalian liver enzyme in terms of substrate requirements and inhibition characteristics.Zimbank. International Program in Chemical Sciences, Uppsala University, Sweden and the Research Board, University of Zimbabwe