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.
Identifer | oai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:uct/oai:localhost:11427/2696 |
Date | January 2005 |
Creators | Mbewe, Boniface |
Contributors | Mcintosh, David B, Chibale, Kelly |
Publisher | University of Cape Town, Faculty of Health Sciences, Division of Chemical Pathology |
Source Sets | South African National ETD Portal |
Language | English |
Detected Language | English |
Type | Doctoral Thesis, Doctoral, PhD |
Format | application/pdf |
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