The expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT)

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dc.contributor.advisorMclntosh, Daviden_ZA
dc.contributor.authorPhehane, Vuyisile Ntosien_ZA
dc.date.accessioned2014-07-28T08:15:16Z
dc.date.available2014-07-28T08:15:16Z
dc.date.issued2002en_ZA
dc.descriptionBibliography: leaves 231-243.
dc.description.abstractWe have expressed and purified human, two forms of P. falciparum, and Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase (HPRT) in E. coli using the pET expression system. The cDNA encoding the ORF of HPRT was amplified by PCR and transformed into E. coli cells using standard methods. Expression was induced by IPTG and reached about 13% of the total cell protein for all four proteins. The HPRTs were purified by nickel affinity chromatography most of the expressed protein could be isolated from the crude supernatant fraction in a soluble form. Human HPRT was active, with activity levels in the region of 38 umoles GMP min⁻¹ mg⁻¹ at 37 ⁰C, which is comparable to published literature values.en_ZA
dc.identifier.apacitationPhehane, V. N. (2002). <i>The expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT)</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology. Retrieved from http://hdl.handle.net/11427/2701en_ZA
dc.identifier.chicagocitationPhehane, Vuyisile Ntosi. <i>"The expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT)."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 2002. http://hdl.handle.net/11427/2701en_ZA
dc.identifier.citationPhehane, V. 2002. The expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT). University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Phehane, Vuyisile Ntosi AB - We have expressed and purified human, two forms of P. falciparum, and Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase (HPRT) in E. coli using the pET expression system. The cDNA encoding the ORF of HPRT was amplified by PCR and transformed into E. coli cells using standard methods. Expression was induced by IPTG and reached about 13% of the total cell protein for all four proteins. The HPRTs were purified by nickel affinity chromatography most of the expressed protein could be isolated from the crude supernatant fraction in a soluble form. Human HPRT was active, with activity levels in the region of 38 umoles GMP min⁻¹ mg⁻¹ at 37 ⁰C, which is comparable to published literature values. DA - 2002 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2002 T1 - The expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT) TI - The expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT) UR - http://hdl.handle.net/11427/2701 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/2701
dc.identifier.vancouvercitationPhehane VN. The expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT). [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 2002 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/2701en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDivision of Chemical Pathologyen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherChemical Pathologyen_ZA
dc.titleThe expression and drug targeting of parasitic hypoxanthine-guanine phosphoribosyltransferase (HGPRT)en_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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