Variation and criteria for generic and specific determination of diphyllobothriid cestodes.
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Chemotaxonomic patterns in the distribution of amino acids of Hymenolepis palmarum (Johri, 1956) and other hymenolepidids revealed the common presence of beta-aminoisobutyric acid, lysine, phenylalanine and tyrosine but 3,4 dihydroxyphenylalanine and norleucine were exclusive to H. palmarum. Both qualitative and quantitative differences in amino acids have been recorded.
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Preparations of isolated brush border plasma membrane of Hymenolepis diminuta and H. microstoma possess the following enzymatic activities: alkaline phosphohydrolase (E.C. 3.1.3.1); Type I phosphodiesterase (E.E. 3.1.4.1); ribonuclease (E.C. 3.1.4.22); adenosine triphosphatase (E.C. 3.6.1.3); and 5'-nucleotidase (E.C. 3.1.3.5). The following enzymatic activities could not be demonstrated in either membrane preparation: Type II phosphodiesterase (E.C. 3.1.4.18); cyclic adenosine-3', 5'-monophosphate phosphodiesterase (E.C. 3.1.4.17); leucine aminopeptidase (E.C. 3.4.11.1); maltase (alpha-glucosidase; E.C. 3.2.1.20); and lactase (beta-galactosidase; E.C. 3.2.1.23). These data generally agree with those of previous studies in which similar membrane-bound enzymes were demonstrated in intact (living) worms.
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