Linked Life Data

6530024

Source:http://linkedlifedata.com/resource/pubmed/id/6530024

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1985-5-16
pubmed:abstractText
The binding of Tb3+ and other lanthanides to Con A has been studied by sensitized Tb3+ luminescence, by quenching of intrinsic fluorescence and by activity measurements. In all the experimental conditions tested, it was found that holo and apo Con A bind lanthanide ions at a site different from the binding sites of the constitutive metals, Mn2+ and Ca2+. The bound lanthanide did not affect the saccharide binding ability and the hemoagglutinating ability of Con A. The intrinsic fluorescence of Con A is quenched by the binding of Tb3+ and Gd3+. The same quenching is obtained by shifting the pH of Con A from pH 6.5 to 4.5. It is proposed that H+ and Ln3+ completely quench a tryptophan, perhaps the residue 88 or 182.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0020-711X
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1409-13
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
A fluorimetric study of the lanthanides binding to concanavalin A.
pubmed:publicationType
Journal Article