Dissertations / Theses on the topic 'Cytochrome C oxidase'
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Howell, T. W. "Reconstituted cytochrome c oxidase vesicles." Thesis, University of Bristol, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.370702.
Full textCappuccio, Jenny A. "Spectroscopic studies of cytochrome c oxidase /." Diss., Digital Dissertations Database. Restricted to UC campuses, 2004. http://uclibs.org/PID/11984.
Full textLin, Jian Chan Sunney I. "ATP modulation of the electron transfer between cytochrome c and cytochrome c oxidase." Diss., Pasadena, Calif. : California Institute of Technology, 1995. http://resolver.caltech.edu/CaltechETD:etd-10182007-085924.
Full textBrändén, Gisela. "Structure and function of cytochrome c oxidase /." Stockholm : Department of Biochemistry and Biophysics, Stockholm University, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1226.
Full textPoynter, D. "Structural studies on bovine heart cytochrome c oxidase." Thesis, University of Nottingham, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356539.
Full textChrzanowska-Lightowlers, Zofia Maria Alexandra. "Regulation of the homeostasis of cytochrome C oxidase." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260970.
Full textAdams, Paula Louise. "Cytochrome c oxidase deficiency : biochemical & molecular studies." Thesis, University of Newcastle Upon Tyne, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337193.
Full textNäsvik, Öjemyr Linda. "Membrane effects on proton transfer in cytochrome c oxidase." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-75633.
Full textSalomonsson, Lina. "Proton, Electron, and O₂ transfer in Cytochrome c Oxidase /." Stockholm : Department of Biochemistry and Biophysics, Stockholm university, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1222.
Full textEl-Agez, Bassam Ali. "A kinetic and spectroscopic study on cytochrome c oxidase." Thesis, University of Essex, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305116.
Full textParet, Claudia. "Assembly of cytochrome c oxidase: the role of hSco1p and hSco2p." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2001. http://nbn-resolving.de/urn:nbn:de:swb:14-1008679017468-62905.
Full textAuclair, Benoît. "Thermosensibilité des propriétés fonctionnelles du complexe cytochrome c oxidase-cytochrome c et coévalution des génomes mitochondrial et nucléaire." Thèse, [Rimouski, Québec] : Université du Québec à Rimouski, 2005.
Find full textTitre de lʹécran-titre (visionné le 31 août 2006). Mémoire présenté à l'Université du Québec à Rimouski comme exigence partielle du programme de maîtrise en gestion de la faune et de ses habitats. CaQRU CaQRU Bibliogr.: f. 55-59. Paraît aussi en éd. imprimée. CaQRU
Namslauer, Ida. "Cytochrome c Oxidase dysfunction in cancer : Exploring the molecular mechanisms." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-65303.
Full textStanley, Brian Allan. "Characterization of cytochrome c oxidase subunit II from Bacillus subtilis." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/MQ63372.pdf.
Full textAlleyne, T. A. "A study of the conformational transitions of cytochrome c oxidase." Thesis, University of Essex, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.235259.
Full textKim, Sun Hee. "Advanced EPR studies of photosystem II and cytochrome c oxidase /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2003. http://uclibs.org/PID/11984.
Full textÄdelroth, Pia. "Mechanisms and pathways for proton transfer in cytochrome-c oxidase." Göteborg : Göteborg University, 1998. http://catalog.hathitrust.org/api/volumes/oclc/68945135.html.
Full textBaden, Katrina Nicolle. "The effects of cytochrome c oxidase deficiency on early development in Danio rerio : a multilevel analysis of pathology /." view abstract or download file of text, 2007. http://proquest.umi.com/pqdweb?did=1417800921&sid=5&Fmt=2&clientId=11238&RQT=309&VName=PQD.
Full textTypescript. Includes vita and abstract. Includes bibliographical references (leaves 70-82). Also available for download via the World Wide Web; free to University of Oregon users.
Williams, Sion Llewelyn. "Aspects of the biogenesis of cytochrome c oxidase in human cells." Thesis, University College London (University of London), 2005. http://discovery.ucl.ac.uk/1446910/.
Full textHartlen, Rebecca. "Expression of cytochrome c oxidase subunit II from a nuclear transgene." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0024/MQ50783.pdf.
Full textLeary, Scot C. "Interactions between bioenergetics and cytochrome c oxidase levels in striated muscles." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ63432.pdf.
Full textLopez, Garcia Roberto. "Bio-mimetic analogues of the active site in cytochrome C oxidase." Thesis, University of Nottingham, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.416397.
Full textPreiss, Thomas. "Cytochrome c oxidase : a model system for post-transcriptional gene regulation." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.281705.
Full textAbubakar, Mohammed Kaoje. "Studies of the structural and functional dynamics of cytochrome c oxidase." Thesis, University of Essex, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.241211.
Full textXu, Shujuan. "EPR studies of electron and proton transfer in cytochrome c oxidase." Diss., Connect to online resource - MSU authorized users, 2008.
Find full textTitle from PDF t.p. (viewed on July 2, 2009) Includes bibliographical references. Also issued in print.
Li, Peter Mark Chan Sunney I. "The role of CuA in the cytochrome c oxidase proton pump /." Diss., Pasadena, Calif. : California Institute of Technology, 1990. http://resolver.caltech.edu/CaltechETD:etd-06202007-085253.
Full textHe, Qizhi Chan Sunney I. Chan Sunney I. "Cytochrome c oxidase : studies of electron input and intramolecular electron transfer /." Diss., Pasadena, Calif. : California Institute of Technology, 1995. http://resolver.caltech.edu/CaltechETD:etd-10052007-085601.
Full textLee, Sang Tae Chemistry Faculty of Science UNSW. "Model studies of the cub-histidine-tyrosine centre in cytochrome c oxidase." Awarded by:University of New South Wales. Chemistry, 2005. http://handle.unsw.edu.au/1959.4/33251.
Full textJohansson, Ann-Louise. "Structural elements involved in protein-mediated proton transfer : Implications from studies of cytochrome c oxidase." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-85934.
Full textAt the time of doctoral defence the following papers were unpublished and had a status as follows: Paper 2: Accepted; Paper 3: Manuscript
Weraarpachai, Woranontee. "Identification and characterization of novel genes involved in cytochrome c oxidase deficiencies." Thesis, McGill University, 2012. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=107626.
Full textDans les mitochondries, l'ATP est généré par la phosphorylation oxydative (PHOSOX), un processus qui nécessite cinq complexes enzymatiques multimériques. Le transport des électrons le long des quatre premiers complexes enzymatiques (complexes I-IV) libère l'énergie qui est stockée sous la forme d'un gradient de protons à travers la membrane interne mitochondriale et est ensuite utilisée par l'ATP synthétase (complexe V) pour produire de l'ATP. Le complexe IV ou cytochrome C oxydase (COX) est l'enzyme terminale de la chaîne respiratoire mitochondriale, catalysant l'oxydation du cytochrome c par l'oxygène moléculaire. Il contient 13 sous-unités structurelles chez les mammifères, dont 3 sont codées par l'ADN mitochondriale. Les déficiences en cytochrome C oxydase peuvent être causées par des mutations dans l'ADN mitochondriale ou l'ADN nucléaire. Les carences en COX peuvent être liées à des mutations dans les sous-unités structurelles ou à des mutations dans des facteurs nécessaires à l'assemblage du complexe enzymatique. Dans cette thèse, deux nouveaux gènes mutés ont été identifiés et caractérisés dans deux patients présentant un déficit en COX. Premièrement, nous avons identifié un défaut spécifique dans la synthèse de la sous-unité COX 1 de l'ADN mitochondriale (COX I) dans un pedigree présentant une apparition tardive du syndrome de Leigh et une carence en COX. Nous avons cartographié le défaut génétique au chromosome 17q par la technique de transfert de chromosomes à médiation microcellulaire. Nous avons, par la suite, identifié une mutation homozygote, une insertion d'une base causant l'apparition prématurée d'un codon stop qui entraîne l'arrêt de la synthèse de la protéine CCDC44, renommé TACO1 pour activateur de la traduction de la COX I. TACO1 est membre d'une famille de protéines contenant un domaine conservé à fonction inconnue, nommé DUF28, qui se localise à la matrice mitochondriale. L'expression de l'ADN complémentaire de type sauvage de TACO1 compense le défaut de traduction de COX I. TACO1 est le premier activateur spécifique de la traduction mitochondriale à être identifié chez les mammifères. Il a été observé que l'absence (knock-down) du gène codant l'orthologue de TACO1 chez la levure, le YGR021w, ne perturbait pas la compétence des voies respiratoires, la traduction mitochondriale, ni l'activité de COX. Ceci suggère que TACO1 a évolué et a acquérit une nouvelle fonction dans la traduction mitochondriale chez les mammifères. Deuxièmement, nous avons étudié une famille dans laquelle le sujet présentait une acidose lactique congénitale et dysmorphie associée à un défaut d'assemblage et une diminution de l'activité enzymatique de la COX due à un défaut spécifique dans la traduction de COX I. En utilisant une combinaison de techniques dont le transfert de chromosomes à médiation microcellulaire, la cartographie d'homozygotie et le profilage de transcription, nous avons cartographié le gène défectueux sur le chromosome 12. Nous avons identifié une mutation faux sens à l'état homozygote provoquant un changement d'acide aminé de méthionine en isoleucine dans le gène C12orf62, un gène qui semble restreint à la lignée des vertébrés. L'expression de l'ADN complémentaire de type sauvage de C12orf62 a restauré la synthèse de COX I et le défaut d'assemblage de la COX. C12orf62 est une très petite protéine transmembranaire (6 kDa), non caractérisée, qui se localise aux mitochondries. Les sous-unités COX I, II et IV co-immunoprécipitent avec un épitope marqué de la protéine C12orf62. Les analyses de bleu d'électrophorèse sur gel de polyacrylamide natif (BN-PAGE) en deux dimensions pour les sous-unités nouvellement synthétisées de la COX mitochondriale ont démontré que la COX assemblée est altérée et que le complexe enzymatique naissant est instable dans les fibroblastes du patient atteint. Nous concluons que C12orf62 est nécessaire pour coordonner les étapes précoces de l'assemblage de la COX et de la synthèse de COX I.
Lemma-Gray, Patrizia. "Structure-function relationships within cytochrome C oxidase and complex I a dissertation /." San Antonio : UTHSC, 2008. http://proquest.umi.com.libproxy.uthscsa.edu/pqdweb?did=1594481111&sid=12&Fmt=2&clientId=70986&RQT=309&VName=PQD.
Full textPawlik, Grzegorz. "Assembly and maturation of cbb3-type cytochrome c oxidase in Rhodobacter capsulatus." Thesis, Strasbourg, 2012. http://www.theses.fr/2012STRAF070.
Full textIn this thesis, the assembly and maturation process of the cbb3-type cytochrome c oxidase (cbb3-Cox) was studied in the purple-non-sulphur phototrophic α-proteobacterium Rhodobacter capsulatus. R. capsulatus contains a highly branched electron-transfer chain and is a well studied model organism for investigating respiratory and photosynthetic processes.The bacteria-specific cbb3-Coxs represent the second most abundant class of cytochrome c oxidases after the aa3-type Cox, but have so far not been investigated in much detail. Recently, the first crystal structure of cbb3-Cox from P. stutzeri was obtained, providing a major breakthrough and inviting detailed studies on the catalytic mechanism and the assembly process. Studies on the assembly and maturation processes are of wide significance due to the fact that many human pathogens like Helicobacter pylori, Neisseria meningitides or Campylobacter jejuni use this type of Cox and it therefore might develop into an attractive drug-target. cbb3-Cox in R. capsulatus is encoded by the ccoNOQP gene operon which codes for four membrane proteins constituting cbb3-Cox. CcoP and CcoO are c-type cytochromes, containing periplasmic heme-binding motifs. CcoN is the central catalytic subunit which contains two b-type hemes and a copper ion. Investigating the delivery of Cu to the CcoN subunit and the assembly of all four subunits into the active cbb3-Cox complex were the main topics of this work. Here the role of the putative assembly factor CcoH, its structure and interaction with cbb3-Cox was investigated in detail. CcoH is a small membrane protein encoded in the ccoGHIS gene cluster located adjacent to the genes coding for cbb3-Cox. In vivo analysis of cbb3-Cox formation in a strain lacking ccoH showed the total absence of cbb3-Cox. Likewise, the stability of CcoH was drastically impaired in a ccoNOQP deletion strain. The mutual dependency of both proteins suggested their direct interaction, which was confirmed by site-directed photocrosslinking of CcoH to the CcoN subunit, by immunodetection of CcoH in cbb3-Cox complexes on Blue Native gels, by CcoH-cbb3-Cox co-purification and by in vitro labelling of cbb3-Cox complexes with radioactively labelled CcoH.[...]
Horn, Darryl M. "Characterization of Two CX9C Containing Mitochondrial Proteins Necessary for Cytochrome c Oxidase Assembly." Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_dissertations/375.
Full textBamji, Michelle. "Functional characterization of the human cytochrome c oxidase factor COX11 using RNA interference." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=81591.
Full textSvahn, Emelie. "Molecular machinery of a membrane-bound proton pump : Studies of charge transfer reactions in cytochrome c oxidase." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2014. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-108335.
Full textPENEDO, Diego Mattos. "An?lise gen?tica e fenot?pica de macacos-prego da Ilha da Marambaia, Mangaratiba, Rio de Janeiro." Universidade Federal Rural do Rio de Janeiro, 2016. https://tede.ufrrj.br/jspui/handle/jspui/1450.
Full textMade available in DSpace on 2017-02-22T20:14:46Z (GMT). No. of bitstreams: 1 2016 - Diego Mattos Penedo.pdf: 4081734 bytes, checksum: 3e13fd4d6f8b8c4d8d31a05fefa2ba14 (MD5) Previous issue date: 2016-02-26
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Several studies have been conducted with capuchin monkeys (Sapajus and Cebus) in order to understand their evolutionary histories by South and Central America. Genetic analysis, in association with the coat coloration, assist in the identification of the relationships between species and show the diversity presented by both genera. In Brazil, Sapajus species are predominantly distributed, being S. nigritus endemic to the Atlantic Forest and characteristic of southeast. At Ilha da Marambaia, an important area with forest remaining in the state of Rio de Janeiro, there is a population of capuchin monkeys, but without previous study. The objective of this study was to characterize the population of capuchin monkeys at this region through phenotypic and genetic analyzes, including the coat coloration, the sequencing of the mitochondrial gene cytochrome oxidase II and the evaluation of karyotype with conventional staining and C-band. Interviews with residents and military personnel in the region, were also carried out, in order to identify the possible origin and isolation of the primates. Twelve specimens, eight males and four females, were analyzed. The coat features were consistent with that described for S. nigritus, with coloration varying from brown to blackish on the back, limbs, tail and top of the head, in addition to yellow chest and face with white or light yellow, contrasting. Tufts at the top of the head were seen in adults, being greater in females. The analysis of mitochondrial gene revealed closer proximity of this population with S. xanthosternos, which occurs at Bahia, and then with S. cay that occurs in parts of Brazil and Paraguay. The greatest divergence was in relation to the population of S. nigritus in Argentina. The karyotype was consistent with that described for Sapajus species, with 2n = 54 (XX or XY), although the morphology of the sex chromosome Y, submetacentric, was different from that commonly described in the literature (acrocentric). Presented intercalary C-band the chromosome pairs 4, 11, 12 and 17. The par 11 presented three polymorphisms, all interstitial to euchromatin and diversified from each other by deletion and inversion processes. The pattern of this pair is different from that described, as a small acrocentric, to S. nigritus in populations of Argentina, with banding similar to that considered specific for S. xanthosternos. According to the survey, the population of primates seems to be native of the island and is currently isolated. According to the genetic divergences found, the population of Ilha da Marambaia may have maintained ancestral characteristics. The C-band pattern of the pair 11 indicates that the polymorphism described for populations of Argentina does not correspond to the entire distribution of S. nigritus. These data may help to understand the diversity and evolution of Sapajus, since this would have radiated from southeastern Brazil. Further studies with populations from other regions of Rio de Janeiro are needed to verify the C-band pattern presented for the pair 11 as well as the genetic relationships demonstrated by the mitochondrial gene for the population of Ilha da Marambaia.
Diversos estudos v?m sendo realizados com macacos-prego e caiararas (Sapajus e Cebus) de modo a entender suas hist?rias evolutivas pelas Am?ricas do Sul e Central. An?lises gen?ticas, em associa??o ?s caracter?sticas de pelagem, auxiliam na identifica??o das rela??es entre as esp?cies e evidenciam a diversidade apresentada por ambos os g?neros. No Brasil, est?o distribu?das predominantemente as esp?cies de Sapajus, sendo S. nigritus end?mica de Mata Atl?ntica e caracter?stica do sudeste. Na Ilha da Marambaia, importante ?rea com remanescente florestal no estado do Rio de Janeiro, existe uma popula??o de macacos-prego, sem nenhum estudo anterior. O objetivo deste trabalho foi caracterizar a popula??o de macacos-prego dessa regi?o atrav?s de an?lises fenot?picas e gen?ticas, incluindo o padr?o de pelagem, o sequenciamento do gene mitocondrial Citocromo Oxidase II e a avalia??o do cari?tipo com colora??o convencional e bandamento de heterocromatina constitutiva (banda C). Foram realizadas, tamb?m, entrevistas com moradores e militares da regi?o, de modo a identificar a poss?vel origem e isolamento dos primatas. Foram analisados doze esp?cimes, oito machos e quatro f?meas. As caracter?sticas de pelagem coincidiram, de modo geral, com descrito para S. nigritus, sendo observada colora??o variando de marrom a enegrecida no dorso, membros, cauda e topo da cabe?a, al?m de peito amarelo e face branca ou amarelo-clara, contrastante. Tufos de pelos no topo da cabe?a foram observados nos adultos, sendo maiores nas f?meas. A an?lise do gene mitocondrial revelou maior proximidade da popula??o da ilha com S. xanthosternos, que ocorre na Bahia, e em seguida com S. cay, que ocorre em parte do Brasil e no Paraguai. A maior diverg?ncia apresentada foi em rela??o a popula??es de S. nigritus da Argentina. A an?lise do cari?tipo revelou padr?o condizente com as esp?cies de Sapajus, com 2n = 54 (XX ou XY), embora a morfologia do cromossomo sexual Y, submetac?ntrica, fosse divergente do comumente descrito na literatura (acroc?ntrica). Apresentaram banda C intercalar os pares cromoss?micos 4, 11, 12 e 17. O par 11 mostrou-se com tr?s polimorfismos, todos intercalares e diversificados entre si por processos de dele??o e invers?o. O padr?o deste par foi divergente do descrito, como um pequeno acroc?ntrico, para S. nigritus em popula??es da Argentina, apresentando bandamento semelhante ao considerado espec?fico de S. xanthosternos. Segundo o levantamento realizado, a popula??o de primatas parece ser natural da ilha, estando provavelmente isolada. De acordo com as diverg?ncias gen?ticas encontradas, a popula??o da Ilha da Marambaia pode ter conservado caracter?sticas ancestrais. O padr?o de banda C do par 11 indica que o polimorfismo descrito para popula??es da Argentina pode n?o corresponder a toda a distribui??o de S. nigritus. Estes dados podem auxiliar no entendimento da diversidade e evolu??o das esp?cies de Sapajus, uma vez que este teria irradiado a partir do sudeste brasileiro. Novos estudos com popula??es de outras regi?es do Rio de Janeiro s?o necess?rios para se averiguar o padr?o de bandamento de heterocromatina apresentada para o par 11, bem como as rela??es gen?ticas demonstradas pelo sequenciamento do gene mitocondrial para a popula??o da Ilha da Marambaia.
Dodia, R. J. "Structure-function relationship of mitochondrial cytochrome c oxidase : redox centres, proton pathways and isozymes." Thesis, University College London (University of London), 2014. http://discovery.ucl.ac.uk/1455977/.
Full textPunnagai, Munusami. "Electrostatic and quantum chemical investigation of the proton pumping mechanism of cytochrome c oxidase." kostenfrei, 2008. http://opus.ub.uni-bayreuth.de/volltexte/2008/475/.
Full textCollins, Jessica M. "FixI and FixI2: Homologous proteins with unique functions in Sinorhizobium meliloti." Digital WPI, 2014. https://digitalcommons.wpi.edu/etd-theses/177.
Full textFisher, Kelli Nicole. "Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism." Wright State University / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=wright1405294648.
Full textCvetkov, Teresa L. "Cytochrome c Oxidase from Rhodobacter sphaeroides: Oligomeric Structure in the Phospholipid Bilayer and the Structural and Functional Effects of a C-Terminal Truncation in Subunit III." Wright State University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=wright1279028849.
Full textMcCann, C. K. "The role of COX4 in the biogenesis of mitochondrial cytochrome c oxidase in Chlamydomonas reinhardtii." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18567/.
Full textLiao, Zhiming. "Molecular aspects of cardiac cytochrome C oxidase and extracellular matrix proteins in copper-deficient rats /." The Ohio State University, 1994. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487853913100837.
Full textIoannidis, Nikolaos. "Intermediate states of mammalian cytochrome c oxidase : the resting/pulsed transition and the oxygen reduction reaction." Thesis, King's College London (University of London), 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.424208.
Full textJanse, van Rensburg Marike. "The role of the cytochrome B and cytochrome C oxidase III genes in the immune response of the South African abalone, Haliotis midae." Master's thesis, University of Cape Town, 2007. http://hdl.handle.net/11427/4275.
Full textIncludes bibliographical references (leaves 80-89).
Although South Africa is the second largest producer of abalone outside Asia, the sustainability of the industry could be threatened by infectious diseases (Troell et ai., 2006). Probiotics are increasingly being viewed as an alternative to chemical and antibiotic treatments (Balcazar et al., 2006), and have been shown to improve the health of the South African abalone, Haliotis midae (Macey and Coyne, 2005). In order to establish better health management systems, and to implement alternative therapies such as probiotics, a better understanding of how the abalone immune system functions, and specifically how it responds to stimulation, is necessary. Two genes of the electron transport system, cytochrome b and cytochrome c oxidase III, were found to be upregulated in a cDNA microarray experiment performed on haemocytes from immunestimulated abalone (Arendze-Bailey, unpublished). The current study sought to confirm these results by semi-quantitative PCR and to further elucidate the roles of these genes, and thus the electron transport system, in the abalone immune response.
Beauchemin, Annie. "Cytochrome c oxidase subunit Vb interacts with human androgen receptor : a potential mechanism for neuronotoxicity in spinobulbar muscular atrophy." Thesis, McGill University, 2000. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=33377.
Full textOur goal was to confirm and further characterize the interaction between hAR and cytochrome c oxidase subunit Vb (COXVb), a nuclear-encoded mitochondrial protein. We had previously isolated COXVb as an AR-interacting protein in a yeast two-hybrid search to identify candidates that interact with normal and polyGln-expanded AR. Using the mammalian two-hybrid system, we confirm that COXVb interacts with normal and mutant AR and demonstrate that the COXVb-normal AR interaction is stimulated by heat shock protein 70 (Hsp70). Also, BFP-tagged AR specifically co-localizes with cytoplasmic aggregates formed by GFP-labelled polyGln-expanded AR in androgen-treated cells.
Mitochondrial dysfunction may precede neuropathological findings in polyGln-expanded disorders and may thus represent an early event in neuronotoxicity. Interaction of COXVb and hAR, with subsequent sequestration of COXVb, may provide a mechanism for putative mitochondrial dysfunction in SBMA.
Oswald, Corina. "Mitochondrial copper homeostasis in mammalian cells." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2010. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-61580.
Full textWhite, Kimberly N. "Syntheses of analogs of the active site of cytochrome[c] oxidase and related new N-methylation metholodgy /." Diss., Digital Dissertations Database. Restricted to UC campuses, 2006. http://uclibs.org/PID/11984.
Full textFaxén, Kristina. "Active transport of ions across biomembranes : a kinetic study of cytochrome c oxidase reconstituted into phospholipid vesicles /." Stockholm : Department of Biochemistry and Biophysics, stockholm university, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-6806.
Full textCoulter, P. D. "Synthetic routes to doubly bridged porphyrins and their use as models for myoglobin and cytochrome c oxidase." Thesis, University of Cambridge, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.377220.
Full text