Pathways of glucose catabolism in procyclic <i>Trypanosoma congolense</i>
NOPR - NISCAIR Online Periodicals Repository
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Title |
Pathways of glucose catabolism in procyclic Trypanosoma congolense
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Creator |
Obungu, Victor H
Kiaira, Job K Olembo, Norah K Njogu, Muturi R |
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Description |
305-311
Studies 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 carboxy kinase, pyruvate dehydrogenase, succinate dehydrogenase, NADP+-linked malic enzyme, ADH fumarate reductase, malate dehydrogenase, and α-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. |
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Date |
2012-12-31T19:58:10Z
2012-12-31T19:58:10Z 1999-10 |
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Type |
Article
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Identifier |
0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15466 |
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Language |
en_US
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Rights |
CC Attribution-Noncommercial-No Derivative Works 2.5 India
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Publisher |
NISCAIR-CSIR, India
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Source |
IJBB Vol.36(5) [October 1999]
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