Proteolytic Enzymes of Pomphorhynchus laevis and in Three Other Acanthocephalan Species

Cystacanths and adults of the acanthocephalan Pomphorhynchus laevis were found to release proteolytic enzymes during in vitro culture. Culture media in which cystacanths had been kept contained a trypsinlike collagenolytic proteinase exhibiting a molecular mass of 29 kDa on gelatin substrate gel ele...

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Bibliographic Details
Published in:The Journal of parasitology 1994-02, Vol.80 (1), p.45-49
Main Authors: Polzer, Martin, Taraschewski, Horst
Format: Article
Language:English
Subjects:
Acanthocephala - enzymology
Acanthocephala - physiology
Animals
Biochemistry-Physiology
Biological and medical sciences
Chromatography, Gel
Copper - pharmacology
Culture media
Culture Media, Conditioned
Electrophoresis
Enzymes
Fish Diseases - parasitology
Fishes
Fundamental and applied biological sciences. Psychology
Gelatins
Gels
Helminthiasis - parasitology
Helminthiasis, Animal
Hydrogen-Ion Concentration
Integument
Invertebrates
Larvae
Less representative or incertae sedis groups: acanthocephala, chaetognatha, gnathostomulida, lophophoria, merostomata, mesozoa, myxozoa, nematorhyncha, pararthropoda, placozoa, priapuloidea, prochordata, pycnogonida, rotifera
Leucyl Aminopeptidase - analysis
Parasite hosts
Parasitism
Parasitology
Peptide Hydrolases - analysis
Serine Proteinase Inhibitors - metabolism
Substrate Specificity
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Summary:Cystacanths and adults of the acanthocephalan Pomphorhynchus laevis were found to release proteolytic enzymes during in vitro culture. Culture media in which cystacanths had been kept contained a trypsinlike collagenolytic proteinase exhibiting a molecular mass of 29 kDa on gelatin substrate gel electrophoresis and a Ph optimum at Ph 9.0. Samples of adults possessed a trypsinlike collagenolytic proteinase with a molecular mass of 26 kDa and showed a Ph optimum at 9.0. Leucine aminopeptidase activity was also present in culture media of adults. An apparent molecular mass of 92 kDa and a Ph optimum at Ph 8.5 were determined for this proteolytic enzyme. It was concluded that the trypsinlike proteinases of both stages were necessary for the complete and quick perforation of the fishes' intestinal wall, whereas the leucine aminopeptidase seemed to have a nutritional function in the terminal stages of protein hydrolysis at the surface of the worm's body wall. Cystacanths of 3 other species of fish-parasitizing Acanthocephala (Acanthocephalus anguillae, Acanthocephalus lucii, Paratenuisentis ambiguus) did not show any histolytic activity.
ISSN:0022-3395
1937-2345
DOI:10.2307/3283343