ISOENZYME VARIATION WITHIN THE GENUS CRYPTOSPORIDIUM

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.