Hepatic Cytosolic Glutathione S- Transferases of ostrich (struthio camelus): partial characterisation and interaction with xenobiotics.
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Date
2015-04-09
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Abstract
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.
Description
An article with pictures.
Keywords
Hepatic cytosolic, Glutathione S-transferases, ostrich, xenobiotics