Isoenzyme variation within the genusCryptosporidium (original) (raw)

Abstract

Soluble extracts of the oocysts of_Cryptosporidium parvum_ had demonstrable, but low, activities of malate dehydrogenase (MDH, EC. 1.1.1.37), carboxylesterase (ES, EC 3.1.1.1) and lactate dehydrogenase (LDH, EC. 1.1.1.27) following thin-layer starch-gel electrophoresis. Much higher activities of glucose phosphate isomerase (GPI, EC. 5.3.1.9) and phosphoglucomutase (PGM, EC. 2.7.5.1) were found, and zymograms of these two enzymes were used to characterise isolates of_C. parvum_ from human, bovine, ovine and cervine sources,C. muris from the brown rat and_C. baileyi_ from young turkeys. PGM and GPI zymograms clearly distinguished between_C. parvum, C. muris_ and_C. baileyi_. The five isolates of_C. parvum_ showed the same electrophoretic mobility for GPI, whereas the PGM mobilitiy of the single human isolate of_C. parvum_ examined was clearly different from that of the other isolates. This is the first report of the use of isoenzymes to distinguish between species and isolates of_Cryptosporidium_.

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Author notes

1. B. W. Ogunkolade
   Present address: University Department of Pharmacology, Mansfield Road, OX1 3QT, Oxford, UK

Authors and Affiliations

1. Department of Clinicial Sciences, London School of Hygiene and Tropical Medicine, Keppel Street, WC1E 7HT, London, UK
   B. W. Ogunkolade, H. A. Robinson & V. McDonald
2. M.A.F.F. Central Veterinary Laboratory, New Haw, KT15 3NB, Surrey, Weybridge, UK
   K. Webster
3. Department of Medical Parasitology, London School of Hygiene and Tropical Medicine, Keppel Street, WC1E 7HT, London, UK
   D. A. Evans

Authors

1. B. W. Ogunkolade
2. H. A. Robinson
3. V. McDonald
4. K. Webster
5. D. A. Evans

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Ogunkolade, B.W., Robinson, H.A., McDonald, V. et al. Isoenzyme variation within the genus_Cryptosporidium_.Parasitol Res 79, 385–388 (1993). https://doi.org/10.1007/BF00931827

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• Received: 16 February 1993
• Accepted: 18 March 1993
• Issue date: May 1993
• DOI: https://doi.org/10.1007/BF00931827

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