Source:http://linkedlifedata.com/resource/pubmed/id/12117500
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2002-7-15
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pubmed:databankReference | |
pubmed:abstractText |
A full-length complementary DNA clone encoding a cytosolic Cu/Zn superoxide dismutase with a M(r) of 15,588 Da was isolated from a Taenia solium larvae complementary DNA library. Comparison analysis of its deduced amino acid sequence revealed a 71% identity with Schistosoma mansoni, 57.2-59.8% with mammalian and less than 54% with other helminth cytosolic Cu/Zn superoxide dismutase. The characteristic motifs and the amino acid residues involved in coordinating copper and zinc enzymatic function are conserved. The T. solium Cu/Zn superoxide dismutase was expressed in the pRSET vector. Enzymatic and filtration chromatographic analysis showed a recombinant enzyme with an activity of 2,941 U/mg protein and a native M(r) of 37 kDa. Inhibition assays using KCN, H(2)O(2), NaN(3) and SDS indicated that Cu/Zn is the metallic cofactor in the enzyme. Thiabendazole (500 microM) and albendazole (300 microM) completely inhibited the activity of T. solium Cu/Zn superoxide dismutase. Thiabendazole had no effect on bovine Cu/Zn superoxide dismutase; in contrast, albendazole had a moderate effect on it at same concentrations. Antibodies against T. solium Cu/Zn superoxide dismutase did not affect the enzymatic function; nevertheless, it cross reacts with several Taenia species, but not with trematodes, nematodes, pig, human and bovine Cu/Zn superoxide dismutase enzymes. Western blot analysis indicated the enzyme was expressed in all stages. These results indicate that T. solium possesses a Cu/Zn superoxide dismutase enzyme that can protect him from oxidant-damage caused by the superoxide anion.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Albendazole,
http://linkedlifedata.com/resource/pubmed/chemical/Anthelmintics,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Thiabendazole
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0020-7519
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1175-82
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12117500-Albendazole,
pubmed-meshheading:12117500-Amino Acid Sequence,
pubmed-meshheading:12117500-Animals,
pubmed-meshheading:12117500-Anthelmintics,
pubmed-meshheading:12117500-Blotting, Western,
pubmed-meshheading:12117500-Cloning, Molecular,
pubmed-meshheading:12117500-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12117500-Molecular Sequence Data,
pubmed-meshheading:12117500-Molecular Weight,
pubmed-meshheading:12117500-Rabbits,
pubmed-meshheading:12117500-Recombinant Proteins,
pubmed-meshheading:12117500-Superoxide Dismutase,
pubmed-meshheading:12117500-Taenia solium,
pubmed-meshheading:12117500-Thiabendazole
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pubmed:year |
2002
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pubmed:articleTitle |
Cloning, production and characterisation of a recombinant Cu/Zn superoxide dismutase from Taenia solium.
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pubmed:affiliation |
Departamento de Microbiología y Parasitología, Facultad de Medicina, Edificio A, 2do piso, Universidad Nacional Autónoma de México, Ciudad Universitaria, Mexico D.F. 04510, Mexico.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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