Classification of Entamoeba Species by Means of Electrophoretic Properties of Amebal Enzymes

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Abstract
Qualitative electrophoretic studies were made on 5 amebal enzymes from 21 cultures of amebae. The enzymes investigated were glucokinase, EC2.7.1.1; glucosephosphate isomerase, EC.5.3.1.9; phosphogluco-mutase, EC.2.7.5.1; malate dehydrogenase (decarboxylating), EC.1.1.1..40; and unclassified enzymes called NADP diaphorase,, A total of 16 different amebal enzyme bands were characterized by direct comparisons on cellulose acetate strips. The amebal enzymes were clearly distinguished from those of the bacterial associate. Ten strains of typical E. histolytica gave r total of 8 characterized enzyme bands, 6 of which were common to all strains. Seven of these strains contained diaphorase d, but not diaphorase e, while in the remaining 3 strains the reverse was found. Five strains of atypical E. histolytica were distinguished from the 10 typical strains by the absence of a 2nd glucokinase band, by the presence of a different isomerase band, and by the absence of a slow-migrating diaphorase band. The enzyme pattern of one of the atypical strains (Huff) was identical with that of E. moshkowskii, the ameba isolated from sewage. Identical enzyme patterns were found for 4 cultures of the reptilian parasites, E. invadens and E. terrapinae. Each gave 7 characterized enzyme bands only one of which was common to E. histolytica and E. moshkowskii.