ISOELECTRIC-FOCUSING OF SOME ENZYMES FROM ECHINOCOCCUS-GRANULOSUS (HORSE AND SHEEP STRAINS) AND ECHINOCOCCUS-MULTILOCULARIS

Extracts of the horse and sheep strains of Echinococcus granulosus and E. multilocularis were compared on the basis of their isoenzyme patterns for 10 enzymes by means of isoelectric focusing in poly-acrylamide gels. The enzymes examined were: acid phosphatase, lactate dehydrogenase, malate de-hydrogenase, malic enzyme, phosphoglucoseisomerase, isocitrate dehydrogenase, adenylate kinase, aldolase and ɑ-glycerophosphate dehydrogenase. Interspecific and intraspecific differences are apparent in the isoenzyme profiles of all the enzymes except adenylate kinase; the pattern and activity of adenylate kinase are identical for both strains of E. granulosus but this enzyme clearly distinguishes these forms from E. multilocularis. The absence of electromorphic variation in any of the enzymes from either form of E. granulosus may be a result of the self-fertilizing hermaphraditism of these organisms. © 1979 Oxford University Press.