Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1987-7-24
pubmed:abstractText
Theoretical consideration is given to the interaction of a bivalent ligand with particulate receptor sites, not only from the viewpoint of quantitatively describing the binding behavior but also from that of the kinetics of ligand release upon infinite dilution of a receptor-ligand mixture. In the latter regard, a general expression is derived that describes the time dependence of the amount of ligand bound as a function of two rate constants for the stepwise dissociation of cross-linked ligand-receptor complex and a thermodynamic parameter expressing the initial ratio of singly linked to doubly linked ligand-receptor complexes. An experimental study of the interaction between Sephadex and concanavalin A is then used to illustrate application of this recommended theoretical approach for characterizing the binding behavior and dissociation kinetics of a bivalent ligand for a system in which all ligand-receptor interactions may be described by a single intrinsic association constant. Published results on the interaction of phosphorylase b with butylagarose are also shown to comply with this simplest model of the bivalent ligand hypothesis; but those for the interaction between immunoglobulin G (IgG) dimers and Fc receptors require modification of the model by incorporation of different intrinsic association constants for the successive binding of receptor sites to the bivalent ligand. These results emphasize the need to consider ligand bivalency as a potential phenomenon in studies of interactions between protein ligands and particulate receptors and illustrate procedures by which the effects of ligand bivalency may be identified and characterized.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Concanavalin A, http://linkedlifedata.com/resource/pubmed/chemical/Dextrans, http://linkedlifedata.com/resource/pubmed/chemical/G(M1) Ganglioside, http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Phosphorylase b, http://linkedlifedata.com/resource/pubmed/chemical/Phosphorylases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Drug, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic, http://linkedlifedata.com/resource/pubmed/chemical/Sepharose, http://linkedlifedata.com/resource/pubmed/chemical/choleragen receptor, http://linkedlifedata.com/resource/pubmed/chemical/sephadex
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1867-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2439115-Animals, pubmed-meshheading:2439115-Cholera Toxin, pubmed-meshheading:2439115-Concanavalin A, pubmed-meshheading:2439115-Dextrans, pubmed-meshheading:2439115-G(M1) Ganglioside, pubmed-meshheading:2439115-Immunoglobulin G, pubmed-meshheading:2439115-Kinetics, pubmed-meshheading:2439115-Ligands, pubmed-meshheading:2439115-Liver, pubmed-meshheading:2439115-Macromolecular Substances, pubmed-meshheading:2439115-Mathematics, pubmed-meshheading:2439115-Phosphorylase b, pubmed-meshheading:2439115-Phosphorylases, pubmed-meshheading:2439115-Rats, pubmed-meshheading:2439115-Receptors, Cell Surface, pubmed-meshheading:2439115-Receptors, Drug, pubmed-meshheading:2439115-Receptors, Fc, pubmed-meshheading:2439115-Receptors, Immunologic, pubmed-meshheading:2439115-Sepharose, pubmed-meshheading:2439115-Thermodynamics
pubmed:year
1987
pubmed:articleTitle
Consequences of ligand bivalency in interactions involving particulate receptors: equilibrium and kinetic studies with Sephadex-concanavalin A, butylagarose-phosphorylase b, and Fc receptor-IgG dimer interactions as model systems.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't