Cytosolic glutathione s-transferases of ostrich liver.
dc.contributor.author | Naik, Yogeshkumar S. | |
dc.contributor.author | Kanyepi, R. | |
dc.contributor.author | Ndiweni, N. | |
dc.contributor.author | Hasler, Julia A. | |
dc.contributor.author | Nyathi, C.B. | |
dc.date.accessioned | 2015-04-09T10:41:21Z | |
dc.date.accessioned | 2023-06-23T14:00:32Z | |
dc.date.available | 2015-04-09T10:41:21Z | |
dc.date.available | 2023-06-23T14:00:32Z | |
dc.date.issued | 2015-04-09 | |
dc.description | An article with 14 pages. | en_US |
dc.description.abstract | 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. | en_US |
dc.description.sponsorship | ZIMBANK, RK Financial from the University of Zimbabwe and International Programs in the Chemical Sciences (Uppsaia, Sweden) | en_US |
dc.identifier.uri | http://196.220.97.103:4000/handle/123456789/496 | |
dc.language.iso | en | en_US |
dc.rights.license | This article was downloaded from NUST Institutional repository, and is made available under the terms and conditions as set out in the Institutional Repository Policy. | en_US |
dc.subject | cytosolic glutathione Stramfmes | en_US |
dc.title | Cytosolic glutathione s-transferases of ostrich liver. | en_US |
dc.type | Article | en_US |
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