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Open Access research which pushes advances in bionanotechnology

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SIPBS is a major research centre in Scotland focusing on 'new medicines', 'better medicines' and 'better use of medicines'. This includes the exploration of nanoparticles and nanomedicines within the wider research agenda of bionanotechnology, in which the tools of nanotechnology are applied to solve biological problems. At SIPBS multidisciplinary approaches are also pursued to improve bioscience understanding of novel therapeutic targets with the aim of developing therapeutic interventions and the investigation, development and manufacture of drug substances and products.

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Comparison of the phosphofructokinase and pyruvate kinase activities of Cryptosporidium parvum, Eimeria tenella and Toxoplasma gondii

Denton, H and Brown, S M and Roberts, C W and Alexander, J and McDonald, V and Thong, K W and Coombs, G H (1996) Comparison of the phosphofructokinase and pyruvate kinase activities of Cryptosporidium parvum, Eimeria tenella and Toxoplasma gondii. Molecular and Biochemical Parasitology, 76 (1-2). pp. 23-29. ISSN 0166-6851

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Abstract

Oocysts of Cryptosporidium parvum were shown to contain a pyrophosphate-dependent phosphofructokinase (PPi-PFK) similar to those previously described for Eimeria tenella and Toxoplasma gondii. PPi-PFK of C. parvum displayed simple hyperbolic kinetics with respect to its substrate fructose 6-phosphate and was not affected by fructose 2,6-bisphosphate, the major allosteric activator of most ATP-PFKs. Inorganic pyrophosphatase was not detectable in any of the three parasites. T. gondii tachyzoites and C. parvum cysts both contained a pyruvate kinase (PK) specific for ADP rather than PPi/AMP. The PK of T. gondii was similar to that of E. tenella in that it displayed strong positive cooperativity with respect to its substrate phosphoenolpyruvate and was heterotropically activated by glucose 6-phosphate, fructose 6-phosphate and fructose 1,6-bisphosphate. PK of C. parvum showed no evidence of allosteric properties. The results suggest that the three coccidia are similar in depending heavily on anaerobic energy production via glycolysis but that the mechanisms for regulating glycolysis are not common to all species.