Abstract
Soluble extracts of the oocysts ofCryptosporidium 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 ofC. parvum from human, bovine, ovine and cervine sources,C. muris from the brown rat andC. baileyi from young turkeys. PGM and GPI zymograms clearly distinguished betweenC. parvum, C. muris andC. baileyi. The five isolates ofC. parvum showed the same electrophoretic mobility for GPI, whereas the PGM mobilitiy of the single human isolate ofC. 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 ofCryptosporidium.
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Ogunkolade, B.W., Robinson, H.A., McDonald, V. et al. Isoenzyme variation within the genusCryptosporidium . Parasitol Res 79, 385–388 (1993). https://doi.org/10.1007/BF00931827
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DOI: https://doi.org/10.1007/BF00931827