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dc.contributor.authorObungu, V H
dc.contributor.authorKiaira, J K
dc.contributor.authorOlembo, N K
dc.contributor.authorNjogu, M R
dc.date.accessioned2013-06-10T14:01:31Z
dc.date.available2013-06-10T14:01:31Z
dc.date.issued1999-10
dc.identifier.citationIndian J Biochem Biophys. 1999 Oct;36(5):305-11en
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/pubmed/10844979
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/30976
dc.description.abstractStudies of respiration on glucose in procyclic Trypanosoma congolense in the presence of rotenone, antimycin, cyanide, salicylhydroxamic acid and malonate have indicated the presence of NADH dehydrogenase, cytochrome b-c1, cytochrome aa3, trypanosome alternate oxidase and NADH fumarate reductase/succinate dehydrogenase pathway that contributes electrons to coenzyme Q of the respiratory chain. The rotenone sensitive NADH dehydrogenase, the trypanosome alternate oxidase, and cytochrome aa3 accounted for 24.5 +/- 6.5, 36.2 +/- 4.2 and 54.1 +/- 5.5% respectively of the total respiration. Activities of lactate dehydrogenase, NAD(+)-linked malic enzyme and pyruvate kinase were less than 6 nanomoles/min/mg protein suggesting that they play a minor role in energy metabolism of the parasite. Phosphoenolpyruvate carboxykinase, pyruvate dehydrogenase, succinate dehydrogenase, NADP(+)-linked malic enzyme, NADH fumarate reductase, malate dehydrogenase, and alpha-ketoglutarate dehydrogenase and glycerol kinase on the other hand had specific activities greater than 60 nanomoles/min/mg protein. These enzyme activities could account for the production of pyruvate, acetate, succinate and glycerol. The results further show that the amount of glycerol produced was 35-48% of the combined total of pyruvate, acetate and succinate produced. It is apparent that some of the glycerol 3-phosphate produced in glycolysis in the presence of salicylhydroxamic acid is dephosphorylated to form glycerol while the rest is oxidised via cytochrome aa3 to form acetate, succinate and pyruvate.en
dc.language.isoenen
dc.publisherUniversity of Nairobi,en
dc.titlePathways of glucose catabolism in procyclic Trypanosoma congolense.en
dc.typeArticleen
local.publisherDepartment of Biochemistry, University of Nairobi, Kenya.en


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