Enzymes of energy metabolism in the bradyzoites and tachyzoites of Toxoplasma gondii
Denton, Helen and Roberts, Craig W. and Alexander, James and Thong, Kam-wah and Coombs, Graham H. (1996) Enzymes of energy metabolism in the bradyzoites and tachyzoites of Toxoplasma gondii. FEMS Microbiology Letters, 137 (1). pp. 103-108. ISSN 0378-1097 (https://doi.org/10.1016/0378-1097(96)00047-X)
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The bradyzoite and tachyzoite forms of Toxoplasma gondii, purified from infected animals, were analysed for their activities of phosphofructokinase, pyruvate kinase, lactate dehydrogenase, NAD(+)- and NADH-linked isocitrate dehydrogenases, and succinic dehydrogenase. Both developmental stages contained high activities of phosphofructokinase (specific for pyrophosphate rather than ATP), pyruvate kinase and lactate dehydrogenase, suggesting that energy metabolism in both forms may centre around a high glycolytic flux linked to lactate production. The markedly higher activity of the latter two enzymes in bradyzoites suggests that lactate production is particularly important in this developmental form. NAD(+)-specific isocitrate dehydrogenase was not detectable in either stage of the parasite (and proved useful as a measure of the purity of the bradyzoite preparation), whereas both parasite forms contained low activities of NADP(+)-linked isocitrate dehydrogenase. The results are consistent with the bradyzoites lacking a functional TCA cycle and respiratory chain and are suggestive of a lack of susceptibility of this developmental stage to atovaquone.
ORCID iDs
Denton, Helen, Roberts, Craig W. ORCID: https://orcid.org/0000-0002-0653-835X, Alexander, James, Thong, Kam-wah and Coombs, Graham H.;-
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Item type: Article ID code: 47344 Dates: DateEvent31 March 1996PublishedSubjects: Medicine > Pharmacy and materia medica
Medicine > Therapeutics. PharmacologyDepartment: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences Depositing user: Pure Administrator Date deposited: 05 Apr 2014 10:14 Last modified: 11 Nov 2024 10:38 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/47344