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dc.contributor.authorOlembo, N K
dc.contributor.authorObungu, V H
dc.contributor.authorKiaira, J K
dc.contributor.authorNjogu, R M
dc.date.accessioned2013-06-10T11:35:25Z
dc.date.available2013-06-10T11:35:25Z
dc.date.issued1999
dc.identifier.citationComp Biochem Physiol B Biochem Mol Biol. 1999 May;123(1):59-65.en
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/pubmed/10425713
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/30707
dc.description.abstractThe effect of various metabolic inhibitors on the rate of oxygen consumption by procyclic culture forms of Trypanosoma congolense utilizing proline as substrate was investigated. Cyanide inhibited the rate of oxygen consumption by 81.0 +/- 6.7%, malonate inhibited the rate by 51.6 +/- 1.6% and Antimycin A by 73.1 +/- 5.9%. A combination of cyanide and malonate inhibited the rate of oxygen consumption by 84.9 +/- 6.7% while a combination of antimycin A and malonate inhibited the rate by 81.6 +/- 7.6%. Rotenone had no effect on the rate of respiration except when the intact cells were first permeabilized by digitonin after which rotenone decreased the rate of respiration by 20-30%. Salicylhydroxamate (SHAM) did not have any effect on the rate of oxygen consumption. Enzymes involved in the catabolism of proline with high activities were: proline dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, fumarase, NADP-linked malic enzyme, alanine aminotransferase and malate dehydrogenase. Activities of 1-pyrroline-5 carboxylate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase and NAD-linked malic enzyme were detectable but lower. The end products of proline catabolism were alanine and glutamate. Unlike the case in Trypanosoma brucei brucei aspartate was not detected. Possible pathways of proline catabolism in procyclic culture forms of T. congolense and of electron transfer are proposeden
dc.language.isoenen
dc.titleCatabolism of proline by procyclic culture forms of Trypanosoma congolense.en
dc.typeArticleen
local.publisherDepartment of Biochemistry, West Virginia University, Morgantown, USAen
local.publisherCollege of health sciences,University of Nairobien


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