Browsing by Author "Kanyepi, R."

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    Cytosolic glutathione s-transferases of ostrich liver.
    (2015-04-09) Naik, Yogeshkumar S.; Kanyepi, R.; Ndiweni, N.; Hasler, Julia A.; Nyathi, C.B.
    Chemicals consummumed by the ostrich are likely to be metabolised by liver detoxifying enzymes such as the cytosolic glutathione Stransferases (GST). We have studied the affinity purified GST from male and female ostrich livers. 1-chloro-2, 4-dinitrobenzene (CDNB) proved to be the best of several substrates tested to measme activity. Activity with this substrate was inhibited by sulphobromoptgnalein and cibamon blue which are well established inhibitors for the m ammalian enzyme. A number of pesticides and environmentai pollutants were also found to be strong inhibitors of the enzymes. Our data indicates that ostrich liver enzymes behave similarly to the mammalian liver enzyme in terms of substrate requirements and inhibition characteristics.
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    Hepatic Cytosolic Glutathione S- Transferases of ostrich (struthio camelus): partial characterisation and interaction with xenobiotics.
    (2015-04-09) Naik, Yogeshkumar S.; Kanyepi, R.; Ndiweni, N.; Nasler, J.A.; Nyathi, C.B.
    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.