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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1977-5-25
|
| pubmed:abstractText |
The binding between cholera toxin or its B-protein subunit and various ganglioside-related oligosaccharides was studied by equilibrium displacement dialysis. At low concentrations of ligand, the binding of monosialo-gangliotetraitol exceeded that of the parent ganglioside II3NeuAcGgOse4-Cer, the possible cell surface receptor for the toxin. The terminal galactose residue and an intact carboxyl group of the sialic acid moiety of monosialo-gangliotetraose were found to be necessary for strong binding to the toxin.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0018-4888
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
358
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
159-63
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1977
|
| pubmed:articleTitle |
Studies of the ligand binding to cholera toxin, II. The hydrophilic moiety of sialoglycolipids.
|
| pubmed:publicationType |
Journal Article
|