Isoelectric focusing of some enzymes from Echinococcus granulosus (horse and sheep strains) and E. 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 polyacrylamide gels. The enzymes examined were: acid phosphatase, lactate dehydrogenase, malate dehydrogenase, malic enzyme, phosphoglucoseisomerase, isocitrate dehydrogenase, adenylate kinase, aldolase and alpha-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.
D000263:Adenylate Kinase / Q000032:analysis; D000818:Animals; D004446:Echinococcus / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000032:analysis; D006736:Horses / Q000469:parasitology; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000032:analysis*; D012756:Sheep / Q000469:parasitology; D013045:Species Specificity
D007527:Isoenzymes; D000263:Adenylate Kinase; D005634:Fructose-Bisphosphate Aldolase