Source:http://linkedlifedata.com/resource/pubmed/id/20801056
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
|
pubmed:dateCreated |
2010-10-26
|
pubmed:abstractText |
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein-ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand binding. A reference ligand (L(ref)), which binds specifically to the protein (P), at the same binding site as the ligand (L) of interest, with known affinity and forms a stable protein-ligand complex in the gas phase, is added to the solution. The fraction of P bound to L(ref), which is determined directly from the ES mass spectrum, is sensitive to the fraction of P bound to L in solution and enables the affinity of P for L to be determined. A mathematical framework for the implementation of the method in cases where P has one or two specific ligand binding sites is given. Affinities of two carbohydrate-binding proteins, a single chain fragment of a monoclonal antibody and the lectin concanavalin A, for monosaccharide ligands are reported and the results are shown to agree with values obtained using isothermal titration calorimetry.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Gases,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Single-Chain Antibodies
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
1879-1123
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 American Society for Mass Spectrometry. Published by Elsevier Inc. All rights reserved.
|
pubmed:issnType |
Electronic
|
pubmed:volume |
21
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1893-9
|
pubmed:meshHeading |
pubmed-meshheading:20801056-Algorithms,
pubmed-meshheading:20801056-Concanavalin A,
pubmed-meshheading:20801056-Gases,
pubmed-meshheading:20801056-Kinetics,
pubmed-meshheading:20801056-Ligands,
pubmed-meshheading:20801056-Monosaccharides,
pubmed-meshheading:20801056-Protein Binding,
pubmed-meshheading:20801056-Single-Chain Antibodies,
pubmed-meshheading:20801056-Spectrometry, Mass, Electrospray Ionization
|
pubmed:year |
2010
|
pubmed:articleTitle |
Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry.
|
pubmed:affiliation |
Alberta Ingenuity Centre for Carbohydrate Science, Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
|
pubmed:publicationType |
Journal Article
|