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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1993-8-12
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pubmed:abstractText |
A receptor for Clostridium difficile toxin A was purified from brush border membranes (BBMs) from the small intestine of infant hamsters. The BBMs were solubilized with Triton X-114, and the solubilized receptor was purified with use of a toxin A immobilized affinity-chromatography column and differential temperature elution. SDS-PAGE and silver staining of the purified receptor revealed numerous high-molecular-weight bands. However, ligand blotting analysis with 125I-toxin A used as the probe identified a 163-kD protein as the predominate toxin A-binding molecule. Toxin A bound to the purified receptor at physiological temperature, but the amount of toxin bound increased at lower temperatures. Bovine thyroglobulin bound to toxin A and inhibited its binding to the purified receptor. Preincubation of the receptor with lectins produced by Bandeirea simplicifolia or Datura stramonium reduced specific binding by 125I-toxin A. Our data indicate that the purified toxin A receptor from small intestine BBMs of infant hamsters is a galactose- and N-acetylglucosamine-containing glycoprotein.
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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/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroglobulin,
http://linkedlifedata.com/resource/pubmed/chemical/tcdA protein, Clostridium difficile
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1058-4838
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
16 Suppl 4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
S219-27
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8324123-Animals,
pubmed-meshheading:8324123-Bacterial Toxins,
pubmed-meshheading:8324123-Binding, Competitive,
pubmed-meshheading:8324123-Carbohydrate Sequence,
pubmed-meshheading:8324123-Chromatography, Affinity,
pubmed-meshheading:8324123-Clostridium difficile,
pubmed-meshheading:8324123-Cricetinae,
pubmed-meshheading:8324123-Enterotoxins,
pubmed-meshheading:8324123-Female,
pubmed-meshheading:8324123-Intestine, Small,
pubmed-meshheading:8324123-Lectins,
pubmed-meshheading:8324123-Male,
pubmed-meshheading:8324123-Membrane Proteins,
pubmed-meshheading:8324123-Mesocricetus,
pubmed-meshheading:8324123-Microvilli,
pubmed-meshheading:8324123-Molecular Sequence Data,
pubmed-meshheading:8324123-Temperature,
pubmed-meshheading:8324123-Thyroglobulin
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pubmed:year |
1993
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pubmed:articleTitle |
Purification of a functional receptor for Clostridium difficile toxin A from intestinal brush border membranes of infant hamsters.
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pubmed:affiliation |
Department of Microbiology, School of Medicine, Texas Tech University Health Sciences Center, Lubbock 79430.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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