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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1976-9-2
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pubmed:abstractText |
The mode of binding of 125I-labelled concanavalin A and succinyl-concanavalin A to rat thymocytes at 4 degrees C was investigated. Simultaneously, the free binding sites of the cell-bound lectin molecules were quantified by horseradish peroxidase binding. Concanavalin A showed cooperative binding while succinyl-concanavalin A did not. The number of molecules of concanavalin A bound to the cell surface when it was saturated was twice the number of molecules of succinyl-concanavalin A. We interpret these results as showing that the binding of native concanavalin A to thymocytes at 4 degrees C brings about a cooperative modification of the membrane which leads to appearance of new receptors. Divalent succinyl-concanavalin A has no such effect. Horseradish peroxidase binding to cell-bound lectin was shown to be related to the immobilization of membrane receptors; the more they are immobilized, the more receptor-associated lectin can bind horseradish peroxidase. This allowed us to establish that post-binding events, which we called micro-redistribution, occurred at 4 degrees C when either concanavalin A or succinyl-concanavalin A binds to cells. A cooperative restriction of the micromobility of cell receptors is produced by increasing concentrations of concanavalin A. Succinyl-concanavalin A does not restrict cell receptor mobility at any concentration tested. The results are discussed in terms of cell stimulation and cell agglutination.
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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/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Horseradish Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Methylmannosides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Drug,
http://linkedlifedata.com/resource/pubmed/chemical/Succinates
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
61-9
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:1278183-Animals,
pubmed-meshheading:1278183-Binding, Competitive,
pubmed-meshheading:1278183-Binding Sites,
pubmed-meshheading:1278183-Concanavalin A,
pubmed-meshheading:1278183-Dose-Response Relationship, Drug,
pubmed-meshheading:1278183-Horseradish Peroxidase,
pubmed-meshheading:1278183-Kinetics,
pubmed-meshheading:1278183-Male,
pubmed-meshheading:1278183-Methylmannosides,
pubmed-meshheading:1278183-Protein Binding,
pubmed-meshheading:1278183-Rats,
pubmed-meshheading:1278183-Receptors, Drug,
pubmed-meshheading:1278183-Succinates,
pubmed-meshheading:1278183-Temperature,
pubmed-meshheading:1278183-Thymus Gland
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pubmed:year |
1976
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pubmed:articleTitle |
Cooperative binding of concanavalin A to thymocytes at 4 degrees C and micro-redistribution of concanavalin A receptors.
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pubmed:publicationType |
Journal Article,
In Vitro
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