Identification and characterization of an {alpha}-mannosidase from Trypanosoma cruzi |
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Authors: | Swanson, Paul M. Carter, Clint E. Hager, Cindy Kim, Wan Joon Obermeier, Sarah Oeltmann, Thomas N. |
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Affiliation: | 1Departments of Medicine and Biochemistry Nashville, TN 37232, USA 2Department of Biology, Vanderbilt University Nashville, TN 37232, USA |
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Abstract: | In this report we describe the first purification and characterizationof the acid -mannosidase from the human parasite Trypanosomacruzi. The purified enzyme exhibited a native mol. wt of 240000 Da and is apparently composed of four identical subunitsof mol. wt 58 000 Da. Each of the four subunits contains oneN-linked high-mannose-type oligosaccharide. The -mannosidaseexhibited a pH optimum of 3.5 and a pI of 5.9. This low pH optimumand the ability of swainsonine to inhibit its activity suggestthat the -mannosidase is a lysosomal enzyme. Antibodies againstthe T.cruzi enzyme did not react with mammalian lysosomal -mannosidaseand, conversely, antibody against a rat lysosomal -mannosidasedid not react with the T.cruzi enzyme. Thus, the T.cruzi enzymeappears to be distinct from its mammalian counterpart. -mannosidase lysosomal enzyme Trypanosoma cruzi |
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