Studies on human protoporphyrinogen oxidase

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dc.contributor.advisorMeissner, Peteren_ZA
dc.contributor.advisorCorrigall, Anneen_ZA
dc.contributor.authorManeli, Mbulelo Hen_ZA
dc.date.accessioned2014-07-29T09:07:12Z
dc.date.available2014-07-29T09:07:12Z
dc.date.issued2002en_ZA
dc.descriptionBibliography: p. 131-170.
dc.description.abstractThis study examines the effects of various protoporphyrinogen oxidase mutations responsible for variegate porphyria, the role of the arginine-59 residue, and the glycines in the conserved flavin binding site, in catalysis and/or cofactor binding. Wild type recombinant human protoporphyrinogen oxidase and a selection of both naturally occurring and self-designed mutants were generated, expresses and purified. The self designed mutants included a conservative and two non-conservative arginine-59 replacements, and substitution of glycine residues at positions 9, 11, and 14 by alanine. The expression and purification for all protoporphyrinogen oxidases was optimised, enabling their purification to homogeneity by single step metal affinity chromatography.en_ZA
dc.identifier.apacitationManeli, M. H. (2002). <i>Studies on human protoporphyrinogen oxidase</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Department of Medicine. Retrieved from http://hdl.handle.net/11427/3424en_ZA
dc.identifier.chicagocitationManeli, Mbulelo H. <i>"Studies on human protoporphyrinogen oxidase."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Department of Medicine, 2002. http://hdl.handle.net/11427/3424en_ZA
dc.identifier.citationManeli, M. 2002. Studies on human protoporphyrinogen oxidase. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Maneli, Mbulelo H AB - This study examines the effects of various protoporphyrinogen oxidase mutations responsible for variegate porphyria, the role of the arginine-59 residue, and the glycines in the conserved flavin binding site, in catalysis and/or cofactor binding. Wild type recombinant human protoporphyrinogen oxidase and a selection of both naturally occurring and self-designed mutants were generated, expresses and purified. The self designed mutants included a conservative and two non-conservative arginine-59 replacements, and substitution of glycine residues at positions 9, 11, and 14 by alanine. The expression and purification for all protoporphyrinogen oxidases was optimised, enabling their purification to homogeneity by single step metal affinity chromatography. DA - 2002 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2002 T1 - Studies on human protoporphyrinogen oxidase TI - Studies on human protoporphyrinogen oxidase UR - http://hdl.handle.net/11427/3424 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/3424
dc.identifier.vancouvercitationManeli MH. Studies on human protoporphyrinogen oxidase. [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Department of Medicine, 2002 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/3424en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDepartment of Medicineen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherMedicineen_ZA
dc.titleStudies on human protoporphyrinogen oxidaseen_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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