{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T12:52:09Z","timestamp":1773665529824,"version":"3.50.1"},"reference-count":31,"publisher":"Cambridge University Press (CUP)","issue":"3","license":[{"start":{"date-parts":[[2009,4,6]],"date-time":"2009-04-06T00:00:00Z","timestamp":1238976000000},"content-version":"unspecified","delay-in-days":5484,"URL":"https:\/\/www.cambridge.org\/core\/terms"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Parasitology"],"published-print":{"date-parts":[[1994,4]]},"abstract":"<jats:title>SUMMARY<\/jats:title><jats:p>In the pathogenesis of sparganosis, proteases have been considered to play important roles in tissue migration and parasite feeding. Several bands of proteolysis were observed when crude extracts of<jats:italic>Spirometra mansoni<\/jats:italic>plerocercoid (sparganum) were examined using gelatin substrate gel at neutral pH, of which two proteases of 198 and 104 kDa were purified by two chromatographic steps, and a 36 kDa protease was purified by gelatin-affinity and DEAE\u2013anion exchange chromatography. All the purified proteases exhibited optimal activity at pH 7\u00b75 and 0\u00b71 M Tris\u2013HCI. Proteolytic activities at 198 and 104 kDa were inhibited specifically by serine protease inhibitors, and 4-(amidinophenyl)methansulfonyl fluoride (APMSF, 0\u00b75 m) and<jats:italic>N<\/jats:italic>-\u03b1\u2013<jats:italic>p<\/jats:italic>\u2013tosyl-L-lysine chloromethyl ketone (TLCK, 1 mM), which strongly suggested that these two proteases were trypsin-like proteases. The activity of the 36 kDa protease was inhibited by<jats:italic>N<\/jats:italic>-tosyl-l-phenylalanine chloromethyl ketone (TPCK, I mM) and chymostatin (0\u00b71 mM), and was potentiated in 10 mM Ca<jats:sup>2+<\/jats:sup>which showed that the protease had a chymotrypsin-like property. All the proteases were Schiff(PAS) positive. Proteases of 198 and 104 kDa degraded collagen completely within 24 h. The 36 kDa enzyme cleaved human recombinant interferon-\u03b3 (rIFN\u03b3) and bovine myelin basic protein. In addition, all the purified proteins elicited strong antibody responses in the infected patients.<\/jats:p>","DOI":"10.1017\/s0031182000076204","type":"journal-article","created":{"date-parts":[[2009,6,5]],"date-time":"2009-06-05T14:01:18Z","timestamp":1244210478000},"page":"359-368","source":"Crossref","is-referenced-by-count":18,"title":["Characterization of three neutral proteases of<i>Spirometra 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