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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1986-7-17
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pubmed:abstractText |
The fluorescence of N-dansylgalactosamine [N-(5-dimethylaminonaphthalene-1-sulphonyl)galactosamine] was enhanced 11-fold with a 25 nm blue-shift in the emission maximum upon binding to soya-bean agglutinin (SBA). This change was used to determine the association constants and thermodynamic parameters for this interaction. The association constant of 1.51 X 10(6) M-1 at 20 degrees C indicated a very strong binding, which is mainly due to a relatively small entropy value, as revealed by the thermodynamic parameters: delta G = -34.7 kJ X mol-1, delta H = -37.9 kJ X mol-1 and delta S = -10.9 J X mol-1 X K-1. The specific binding of this sugar to SBA shows that the lectin can accommodate a large hydrophobic substituent on the C-2 of galactose. Binding of non-fluorescent ligands, studied by monitoring the fluorescence changes when they are added to a mixture of SBA and N-dansylgalactosamine, indicates that a hydrophobic substituent at the anomeric position increases the affinity of the interaction. The C-6 hydroxy group also stabilizes the binding considerably. Kinetics of binding of N-dansylgalactosamine to SBA studied by stopped-flow spectrofluorimetry are consistent with a single-step mechanism and yielded k+1 = 2.4 X 10(5) M-1 X s-1 and k-1 = 0.2 s-1 at 20 degrees C. The activation parameters indicate an enthalpicly controlled association process.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-1259427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-13067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-17738723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-17812054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-356549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-375217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-4332414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-4376331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-4517665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-4855992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-6070843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-6174855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-620810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-6313203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-6547140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-6726799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-6893288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-7023359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-7215338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-7260053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-7410420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3755041-913420
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
234
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
515-22
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:3755041-Acetylgalactosamine,
pubmed-meshheading:3755041-Carbohydrate Metabolism,
pubmed-meshheading:3755041-Dansyl Compounds,
pubmed-meshheading:3755041-Fluorescent Dyes,
pubmed-meshheading:3755041-Galactosamine,
pubmed-meshheading:3755041-Kinetics,
pubmed-meshheading:3755041-Lectins,
pubmed-meshheading:3755041-Plant Lectins,
pubmed-meshheading:3755041-Soybean Proteins,
pubmed-meshheading:3755041-Soybeans,
pubmed-meshheading:3755041-Spectrometry, Fluorescence,
pubmed-meshheading:3755041-Thermodynamics
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pubmed:year |
1986
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pubmed:articleTitle |
Thermodynamic and kinetic studies on saccharide binding to soya-bean agglutinin.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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