Glutathione Transferase of Schistoma Mansoni and its Interaction with Praziquantel.

dc.contributor.authorHasler, Julia A.
dc.date.accessioned2013-03-11T06:30:29Z
dc.date.accessioned2023-06-26T12:55:36Z
dc.date.available2013-03-11T06:30:29Z
dc.date.available2023-06-26T12:55:36Z
dc.date.issued2013-03-11
dc.descriptionPresented at the Research Day Seminar 1990, University of Zimbabween_US
dc.description.abstractGlutathione S-transferases play an important role in the excretion of xenobiotics as well as in the antioxidant defence system of cells. The glutathione S-transferase of the parasitic' trematode Schistosoma mansoni has been studied. The results of preliminary experiments are presented here. The pH optimum of the enzyme was found to be 9.5 which is much higher than that of the mammalian liver enzyme. The apparent Km for the substrate 1 chloro 2,4 dinitrobenzene (CDNBL was 1.25 mN and for glutathione was 0.37 roM. The antischistosomal drug Praziquantel was found to inhibit the conjugation of CDNB in a competitive manner. The implications of these results will be discussed.en_US
dc.identifier.urihttp://196.220.97.103:4000/handle/123456789/246
dc.language.isoenen_US
dc.rights.licenseThis 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.subjectGlutathioneen_US
dc.subjectTransferaseen_US
dc.subjectSchistoma Mansonien_US
dc.subjectPraziquantelen_US
dc.titleGlutathione Transferase of Schistoma Mansoni and its Interaction with Praziquantel.en_US
dc.typePresentationen_US
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