title: Purification and partial characterization of proteinase activity in eggs of Dicrocoelium dendriticum.
abstract: 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.
authors.affiliation: Parasitology Laboratory, Faculty of Pharmacy, Alcalá University, Alcalá de Henares, Madrid, Spain. consuelo.gimenez@uah.es.
authors.forename: C
authors.initials: C
authors.lastname: Giménez-Pardo
authors.forename: C
authors.initials: C
authors.lastname: de Armas-Serra
authors.forename: F
authors.initials: F
authors.lastname: Rodríguez-Caabeiro
mesh_terms: D000818:Animals; D001391:Azo Compounds / Q000737:chemistry; D003094:Collagen / Q000737:chemistry; D004396:Coloring Agents / Q000737:chemistry; D004013:Dicrocoelium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010063:Ovum / Q000201:enzymology*; D012756:Sheep / Q000469:parasitology
chemical_list: D001391:Azo Compounds; D004396:Coloring Agents; C028470:Azocoll; D003094:Collagen; D010450:Endopeptidases