PMID: 2092301Dec 1, 1990Paper

Hymenolepis diminuta (Cestoda) liberates an inhibitor of proteolytic enzymes during in vitro incubation

Parasitology
P W Pappas, G L Uglem

Abstract

Hymenolepis diminuta liberated measurable amounts of 'Lowry-positive material' (LPM) and protein during incubation for 2 h in vitro. When tapeworms were incubated in the presence of bovine trypsin (BT), or when BT was added to the medium after removing the tapeworms, the enzyme's proteolytic activity was inhibited significantly. Centrifugation of the medium at 30,000 g yielded a pellet composed of tegumental elements, but this fraction did not inhibit BT. The 30,000 g supernatant fraction contained a chemical(s) that inhibited the proteolytic enzymes of the rodent host's intestinal contents (IC). The inhibitor(s) was stable following repeated freeze-thaw cycles, heat labile, and not degraded by BT or IC, and it inhibited the amidase activity of BT in a non-competitive manner.

References

Mar 1, 1979·Journal of Medical Ethics·J S SturgesD Pickar
Dec 1, 1972·The Biological Bulletin·P W Pappas, C P Read
Mar 1, 1974·Neuropsychologia·A L BentonM W Van Allen
Jun 1, 1971·Experimental Parasitology·D F Mettrick
Dec 1, 1983·Archives of Gerontology and Geriatrics·F A PisantiE Vuttariello
Apr 1, 1980·The Journal of Physiology·J H KoeslagA W Sloan
Dec 30, 1963·Annals of the New York Academy of Sciences·C P READJ E SIMMONS

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Citations

Sep 2, 2017·Doklady Biological Sciences : Proceedings of the Academy of Sciences of the USSR, Biological Sciences Sections·G I IzvekovaT V Frolova
Jun 1, 2017·Folia Parasitologica·Galina I IzvekovaEvgeny I Izvekov

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