Isolation and partial characterization of a Taenia taeniaeformis metacestode proteinase inhibitor |
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Authors: | C Suquet C Grben-Edwards RWes Leid |
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Institution: | 1. Department of Veterinary Microbiology/Pathology, Washington State University, Pullman, WA 99164, U.S.A.;2. formerly of the Department of Pathology, Michigan State University, East Lansing, MI 48824, U.S.A. |
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Abstract: | Suquet C., Green-Edwards C. and Wes Leid R. 1984. Isolation and partial characterization of a Taenia taeniaeformis metacestode proteinase inhibitor. International Journal for Parasitology14: 165–172. A proteinase inhibitor from the metacestode of Taenia taeniaeformis was purified 136-fold to apparent homogeneity as evidenced by one Coomassie Blue protein staining band on 10% SDS slab gels under both reducing and non-reducing conditions. The apparent molecular weight under dissociating conditions was 19,500. This parasite protein inhibited esterolysis of TAME and BTEE by bovine pancreatic trypsin and chymotrypsin respectively in a time and dose-dependent manner. Proteolysis of casein by both enzymes was also inhibited in a time and dose-dependent manner. The parasite inhibitor was stable from pH 2.2 to 10.5 and was fully active after heating at 56 °C for 3 h. The proteases pronase and thermolysin, at concentrations of 1 mg ml?1, completely inactivated the metacestode inhibitor. Two sulfhydryl proteases, papain and chymopapain, used at concentrations of 1 mg ml?1 were without effect. The irreversible proteinase inhibitors TLCK, TPCK and PMSF at concentrations up to 10 mM had no effect on the parasite inhibitor. |
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Keywords: | metacestode proteinase inhibitor larval cestodes longterm survival trypsin inhibition chymotrypsin inhibition esterolysis proteolysis |
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