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. 1987 Dec;62(4):629–634.

Characterization and mast cell origin of a chymotrypsin-like proteinase isolated from intestines of mice infected with Trichinella spiralis.

G F Newlands 1, S Gibson 1, D P Knox 1, R Grencis 1, D Wakelin 1, H R Miller 1
PMCID: PMC1454160  PMID: 3323034

Abstract

A proteinase was purified by cation exchange and affinity chromatography from the small intestines of mice infected with Trichinella spiralis. The enzyme was highly soluble and was chymotrypsin-like in its substrate specificities and susceptibility to inhibitors. It had a MW of 26,000, as determined by SDS-PAGE electrophoresis. Antibodies raised against the proteinase were affinity purified and their specificity confirmed by Western blot analysis. When used to localize the enzyme immunohistochemically, they reacted with granules of mast cells in the epithelium and lamina propria of the parasitized small intestine. The antibodies also bound to mast cell granules in a number of other sites, including tracheal epithelium, gastric mucosa, skin and tongue. Affinity-purified antibodies raised against rat mast cell proteinase II (RMCPII) cross-reacted with the mouse mast cell proteinase on Western blots.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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