Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)

Includes bibliographical references. === The research concerns sub-cloning the gene for HGXPRT from Plasmodium falciparum from a vector with a His-tag facility to one without, expression of the protein in E. coli, and purification. On an analytical scale (40 ml culture), a purification procedure was...

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Main Author:	Mbewe, Boniface
Other Authors:	Mcintosh, David B
Format:	Doctoral Thesis
Language:	English
Published:	University of Cape Town 2014
Subjects:	Chemical Pathology
Online Access:	http://hdl.handle.net/11427/2696

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spelling	ndltd-netd.ac.za-oai-union.ndltd.org-uct-oai-localhost-11427-26962020-07-22T05:07:54Z Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT) Mbewe, Boniface Mcintosh, David B Chibale, Kelly Chemical Pathology Includes bibliographical references. The research concerns sub-cloning the gene for HGXPRT from Plasmodium falciparum from a vector with a His-tag facility to one without, expression of the protein in E. coli, and purification. On an analytical scale (40 ml culture), a purification procedure was developed that involves extraction of contaminating proteins by anion exchange chromatography (HGXPRT does not bind under the conditions used), followed by Reactive Red 120 agarose affinity chromatography. 2014-07-28T08:14:03Z 2014-07-28T08:14:03Z 2005 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/2696 eng application/pdf University of Cape Town Faculty of Health Sciences Division of Chemical Pathology
collection	NDLTD
language	English
format	Doctoral Thesis
sources	NDLTD
topic	Chemical Pathology
spellingShingle	Chemical Pathology Mbewe, Boniface Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)
description	Includes bibliographical references. === The research concerns sub-cloning the gene for HGXPRT from Plasmodium falciparum from a vector with a His-tag facility to one without, expression of the protein in E. coli, and purification. On an analytical scale (40 ml culture), a purification procedure was developed that involves extraction of contaminating proteins by anion exchange chromatography (HGXPRT does not bind under the conditions used), followed by Reactive Red 120 agarose affinity chromatography.
author2	Mcintosh, David B
author_facet	Mcintosh, David B Mbewe, Boniface
author	Mbewe, Boniface
author_sort	Mbewe, Boniface
title	Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)
title_short	Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)
title_full	Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)
title_fullStr	Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)
title_full_unstemmed	Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)
title_sort	cloning, expression, purification and drug targeting of plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (hgxprt)
publisher	University of Cape Town
publishDate	2014
url	http://hdl.handle.net/11427/2696
work_keys_str_mv	AT mbeweboniface cloningexpressionpurificationanddrugtargetingofplasmodiumfalciparumhypoxanthineguaninexanthinephosphoribosyltransferasehgxprt
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Cloning, expression, purification and drug targeting of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (HGXPRT)

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