ABSTRACT
Five clones of axenic E. histolytica (HMI) grown as discrete colonies in semisolid agar medium were adapted in liquid medium and labelled as HMI-C121, HMI-C131, HMI-C143, HMI-C144 and HMI-C145. Isoenzymes of these 5 clones of E. histolytica (HMI) were investigated in starch gel electrophoresis. There were no differences in the electromobility of maleate NADP oxidoreductase and glucosephosphoisomerase amongst the five clones and uncloned cultures of axenic E. histolytica. The relative electromobility (rf) of a single phosphoglucomutase (PGM) band of uncloned Mexican E. histolytica (HMI) and Indian axenic E. histolytica (KCG: 0986: 11) cultures and cloned E. histolytica HMI-C121, HMI-C145 was 0.087 while a single PGM band of uncloned E. histolytica (NIH: 200) and cloned E. histolytica HMI-C131, HMI-C143 and HMI-C144 cultures had rf of 0.075. Isoenzyme characterization of four cloned HMI-C121, HMI-C131, HMI-C143, HMI-C144 cultures of axenic E. histolytica (HMI) revealed existence of three bands of hexokinase (HK). The additional third band of HK was located close to the place of application of lysate and had rf ranging from 0.11-0.14. The data indicated that parent axenic E. histolytica (HMI) consisted of several populations and each population expressed different isoenzyme pattern without an association of amoebic cultures with any bacterial species.