Vazquez-Lopez C ; de Armas-Serra C ; Gimenez-Pardo C ; Rodriguez-Caabeiro F ;

Parasitol Res vol. 85 (1)   pp. 64-70, Jan 1999

Laboratory of Parasitology, Faculty of Pharmacy, University of Alcala, Alcala de Henares, Madrid, Spain.

The present report demonstrates that the Gymnorhynchus gigas plerocercoid possesses various types of endo- and exoproteases with activity against general (azocoll, azocasein, and azoalbumin) and specific substrates (elastin, keratin, collagen, hemoglobin, fibrinogen, plasma, and immunoglobulin G). The activity against collagen is principally due to a 24-kDa collagenase with an isoelectric point of 7.5 and without isoforms or sugar residues. Moreover, its high degree of proteolytic activity against collagen under conditions similars to those encountered by the parasite in its hosts (pH and temperature) and its similarity to metallo- and cysteine proteases (the principal protease types implicated in degradation of tissues) suggests the importance of this molecule as a lytic enzyme principally implicated in penetration processes across the teleost muscle or/and into the gastrointestinal system of elasmobranch fishes as well as in molting processes.

Animal ;  Cestoda: enzymology: isolation & purification ;  Collagenases: isolation & purification: metabolism ;  Electrophoresis,Polyacrylamide Gel ;  Fishes: parasitology ;  Glycosylation ;  Isoelectric Focusing ;  Kinetics ;  Molecular weight ;  Protease Inhibitors: pharmacology ;  Substrate specificity ;  Swine ;  4450 ;