Abstract：
: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.
journal_name
Parasitol Resjournal_title
Parasitology researchauthors
Vázquez-López C,de Armas-Serra C,Giménez-Pardo C,Rodríguez-Caabeiro Fdoi
10.1007/s004360050508subject
Has Abstractpub_date
1999-01-01 00:00:00pages
64-70issue
1eissn
0932-0113issn
1432-1955journal_volume
85pub_type
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