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dc.rights.licenseAl consultar y hacer uso de este recurso, está aceptando las condiciones de uso establecidas por los autores.es_CO
dc.contributor.advisorZimmermann, Barbara Hanna
dc.contributor.authorHortua Triana, Miryam Andrea
dc.date.accessioned2018-09-27T16:38:01Z
dc.date.available2018-09-27T16:38:01Z
dc.date.issued2010
dc.identifier.urihttp://hdl.handle.net/1992/7764
dc.descriptioniles_CO
dc.descriptionIncluye referencias bibliográficas /h. 62-75)es_CO
dc.descriptionExiste copia en microfichaes_CO
dc.description.abstractThe pyrimidine biosynthesis patway in the protozoan pathogen Toxoplosma gondii is essenial for parasite growth during infection. To investigate the properties of Dihydroorotate dehydrogenase (TgDHOD. TgDHOD exhibited a specific activity of 83.8 U/mg, a kcat of 89.2 sec-1 ± 1.5. a Km = 60.3 ±0.002 æM for L-dihydroorotate, and a Km = 28.9 æM ± 1.8 for decylubiquinone (QD). Quinones lacking or having short isoprenoid side chains yielded lower kcats and higher Kms than QD. As expected, fumarate was a poor electron acceptor for this family 2 DHOD. The determined for Redoxal and A77-1726 were 253.3 æM ± 13.3 and 91.2 æM ±2.2, respectively. The enzyme was not significantly affected by brequinar or TTFA, known inhibitors of human DHOD, or by atovaquone. TgDHOD exhibits a 157 ? residue N-terminal extension, consistent with potential organellar targeting, but bioinformatic analysis failed to reveal a consensus subcellular destination, Preliminary inmunolocalization studies of TgDHOD performed in intra- and extracellular parasites treated with the polyclonal antibodies raised against purified recombinant TgDHOD exhibited fluorescence that appeared to colocalize with the apicoplast in fluorescence was observed in -10% of mitochondria stained with Mitotracker Red in extracellular parasites. These findings suggest that TgDHOD is associated with both the apicoplast and mitochondrion, making it a member of a growing list of a metabolic enzymes that are dual targeted in T. gondiies_CO
dc.format.extent83 hes_CO
dc.language.isoenges_CO
dc.publisherBogotá - Uniandeses_CO
dc.sourceinstname:Universidad de los Andeses_CO
dc.sourcereponame:Sénecaes_CO
dc.titleDihydroorotate dehydrogenase of Toxoplasma gondii - kinetic characterization and intracellular localizationes_CO
dc.typedoctoralThesises_CO
dc.publisher.programDoctorado en Ciencias - Biologíaes_CO
dc.rights.accessRightsopenAccess
dc.subject.keywordDihydroorotate dehydrogenase - Investigacioneses_CO
dc.subject.keywordToxoplasma gondii - Investigacioneses_CO
dc.subject.keywordPirimidinas - Biosíntesis - Investigacioneses_CO
dc.subject.keywordPlástidos - Investigacioneses_CO
dc.creator.degreeTesis (Doctor en Ciencias - Biología) -- Universidad de los Andeses_CO
dc.identifier.urlhttp://biblioteca.uniandes.edu.co/acepto220102.php?id=658es_CO
dc.publisher.facultyFacultad de Cienciases_CO
dc.publisher.departmentDepartamento de Biologíaes_CO
dc.type.versionpublishedVersion


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