{"id":{"repo_id":"cape-town","oai_identifier":"oai:open.uct.ac.za:11427/3424"},"canonical_url":"https://search.dev.ndltd.org/etd/cape-town/oai:open.uct.ac.za:11427/3424","repository":{"repo_id":"cape-town","name":"University of Cape Town","base_url":"https://open.uct.ac.za/oai/request"},"display":{"title":"Studies on human protoporphyrinogen oxidase","abstract":"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.","abstract_html":"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.","abstract_has_math":false,"creators":["Maneli, Mbulelo H"],"institution":"Department of Medicine","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Meissner, Peter","Corrigall, Anne"],"committee_chairs":[],"committee_members":[],"year":2002,"date_issued":"2002","date_published":"2002","updated_at":"2026-07-22T22:23:24Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11427/3424","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Meissner, Peter","Corrigall, Anne"]},{"key":"dc:creator","label":"Author","values":["Maneli, Mbulelo H"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-07-29T09:07:12Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-07-29T09:07:12Z"]},{"key":"dc:date.issued","label":"Date","values":["2002"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Department of Medicine"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Cape Town"]},{"key":"dc:type","label":"Dc Type","values":["Doctoral Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["Doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["PhD"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11427/3424"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Bibliography: p. 131-170."]},{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:title","label":"Title","values":["Studies on human protoporphyrinogen oxidase"]}]}],"canonical_facts":{"dc:contributor.advisor":["Meissner, Peter","Corrigall, Anne"],"dc:creator":["Maneli, Mbulelo H"],"dc:date.accessioned":["2014-07-29T09:07:12Z"],"dc:date.available":["2014-07-29T09:07:12Z"],"dc:date.issued":["2002"],"dc:description":["Bibliography: p. 131-170."],"dc:description.abstract":["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."],"dc:identifier.uri":["http://hdl.handle.net/11427/3424"],"dc:language.iso":["eng"],"dc:publisher.department":["Department of Medicine"],"dc:publisher.institution":["University of Cape Town"],"dc:title":["Studies on human protoporphyrinogen oxidase"],"dc:type":["Doctoral Thesis"],"dc:type.qualificationlevel":["Doctoral"],"dc:type.qualificationname":["PhD"]},"updated_at":"2026-07-22T22:23:24Z"}