Source:http://linkedlifedata.com/resource/pubmed/id/12760631
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2003-5-22
|
| pubmed:abstractText |
We produced the Taenia solium triosephosphate isomerase (TPI) in Escherichia coli and compared its biochemical and immunological properties with those of the commercial TPI from Sus scrofa. Taenia solium TPI is a homodimer composed of two 27-kDa monomers, with a specific activity of 5,683 U/mg and a Km value of 0.758, and S. scrofa TPI is also dimeric with similar monomeric molecular weight, specific activity of 4,227 U/mg, and a Km value of 0.51. The catalytic parameters for the isomerization of glyceraldehyde 3-phosphate, affinity between TPI monomers, and kinetic thermal denaturation and inactivation were similar for both enzymes. Anti-T. solium TPI antibodies cross-react weakly with Schistosoma mansoni TPI but do not cross-react with S. scrofa, human, or protozoan TPIs. These antibodies inhibited T. solium TPI activity but did not affect S. scrofa enzymatic activity. Immunizations with 1 microg of the T. solium TPI reduced 52% of cysticerci in a mouse-Taenia crassiceps model 1 mo after challenge. Our findings show that T. solium and S. scrofa TPIs possess similar biochemical and enzymatic properties but do not share immunological properties because anti-T. solium TPI antibodies did not recognize S. scrofa TPI. Inhibition of enzyme activity by anti-TPI antibodies suggests that they can be used as inhibitors of the enzyme.
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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/Antibodies, Helminth,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Helminth,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Triose-Phosphate Isomerase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
|
| pubmed:issn |
0022-3395
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
89
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
209-14
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:12760631-Animals,
pubmed-meshheading:12760631-Antibodies, Helminth,
pubmed-meshheading:12760631-Antigens, Helminth,
pubmed-meshheading:12760631-Blotting, Western,
pubmed-meshheading:12760631-Chromatography, Gel,
pubmed-meshheading:12760631-Circular Dichroism,
pubmed-meshheading:12760631-Cysticercosis,
pubmed-meshheading:12760631-Disease Models, Animal,
pubmed-meshheading:12760631-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12760631-Helminth Proteins,
pubmed-meshheading:12760631-Hot Temperature,
pubmed-meshheading:12760631-Immune Sera,
pubmed-meshheading:12760631-Mice,
pubmed-meshheading:12760631-Protein Folding,
pubmed-meshheading:12760631-Rabbits,
pubmed-meshheading:12760631-Recombinant Proteins,
pubmed-meshheading:12760631-Swine,
pubmed-meshheading:12760631-Taenia solium,
pubmed-meshheading:12760631-Triose-Phosphate Isomerase
|
| pubmed:year |
2003
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| pubmed:articleTitle |
A comparative study of biochemical and immunological properties of triosephosphate isomerase from Taenia solium and Sus scrofa.
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| pubmed:affiliation |
Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, Edificio A, 2 Piso, Ciudad Universitaria, México DF 04510, México.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|