PMID: 9557800Apr 29, 1998Paper

The isolation and purification of a dual specific mast cell-derived protease from parasitised caprine jejunal tissue

Research in Veterinary Science
C N MacaldowieJ F Huntley

Abstract

A mast cell granule protease has been isolated and purified from nematode-infected caprine jejunal homogenate by FPLC techniques and termed Goat Mast Cell Protease (GMCP). The purification steps were monitored for proteolytic activity against the synthetic substrate carboxybenzoyl-L-lysine thiobenzyl ester (BLT) and the presence of a homogenous protease preparation in the final sample was shown by SDS-PAGE electrophoresis. This protease was compared with enzymatic activity from isolated mucosal mast cells, which demonstrated the putative mast cell-derived source of the purified enzyme. Rabbit antiserum was raised against the protease and through the use of immunohistochemistry and Western blotting techniques the mast cell origin of the protease was confirmed. NH2-Terminal amino acid sequence analysis demonstrated a high degree of homology between GMCP and other previously isolated mast cell proteases including sheep mast cell protease (SMCP). Substrate analysis showed that GMCP also had an unusual dual chymotrypsin-like and trypsin-like activity similar to SMCP and bovine duodenase.

References

Apr 1, 1976·Australian Veterinary Journal·L F Le Jambre, W M Royal
Nov 1, 1992·Journal of Comparative Pathology·J F Huntley
Jul 1, 1992·International Journal for Parasitology·W O JonesD L Emery
Jan 10, 1989·Biochemistry·H L TrongR G Woodbury
Jan 1, 1986·The International Journal of Biochemistry·J F HuntleyH R Miller
Sep 1, 1987·Parasite Immunology·J F HuntleyH R Miller
Jan 1, 1986·The International Journal of Biochemistry·D P KnoxJ F Huntley
Jan 1, 1966·Acta Pathologica Et Microbiologica Scandinavica·L Enerbäck
Feb 1, 1995·European Journal of Biochemistry·T S ZamolodchikovaV K Antonov
Feb 1, 1996·International Journal for Parasitology·D M PattersonA J Russel

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