Purification and partial characterization of proteinase activity in eggs of Dicrocoelium dendriticum

A preliminary purification has been carried out by continuous elution electrophoresis of a 49.5 kDa protease of crude extracts from Dicrocoelium dendriticum eggs. The enzyme showed a high capacity to degrade the collagen derivative azocoll at acidic pH. Although it is necessary to carry out further...

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Veröffentlicht in:	Journal of helminthology 2001, Vol.75 (1), p.57-59
Hauptverfasser:	Giménez-Pardo, C., Armas-Serra, C. de, Rodríguez-Caabeiro, F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Azo Compounds - chemistry Biological and medical sciences Collagen - chemistry Coloring Agents - chemistry Dicrocoelium - enzymology Electrophoresis, Polyacrylamide Gel Endopeptidases - isolation & purification Endopeptidases - metabolism Fundamental and applied biological sciences. Psychology Host parasite relation pathogenicity Hydrogen-Ion Concentration Invertebrates Nemathelminthia. Plathelmintha Ovum - enzymology Sheep - parasitology
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Zusammenfassung:	A preliminary purification has been carried out by continuous elution electrophoresis of a 49.5 kDa protease of crude extracts from Dicrocoelium dendriticum eggs. The enzyme showed a high capacity to degrade the collagen derivative azocoll at acidic pH. Although it is necessary to carry out further experiments to confirm any physiological role, this protease could be implicated in penetration mechanisms.
ISSN:	0022-149X 1475-2697
DOI:	10.1079/JOH200035