Dissociation kinetics of bivalent ligand-immunoglobulin e aggregates in solution

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Abstract

We study the dissociation of preformed bivalent ligand-bivalent receptor aggregates in solution, where the ligand is a symmetric bivalent hapten with two identical 2,4-dinitrophenyl (DNP) groups and the receptor is a fluorescein-labeled monoclonal anti-DNP IgE. We promote dissociation in two ways: by the addition of high concentrations of a monovalent hapten that competes for IgE binding sites with the bivalent hapten and by the addition of high concentrations of unlabeled IgE that binds almost all ligand binding sites that dissociate from labeled IgE. We investigate both theoretically and experimentally the two types of dissociation and find them to be quite different. Theory predicts that their kinetics will depend differently on the fundamental rate constants that characterize binding and aggregation. Using monovalent ligand to promote dissociation, we find that the fraction of labeled IgE sites bound to bivalent ligand decays with a slow and fast component. The fast decay corresponds to the dissociation of a singly bound DNP hapten. The interpretation of the slow decay depends on the detailed way in which ligand-receptor aggregates break up. We show that one possible explanation of these data is that small stable rings form before the addition of monovalent ligand. Other possible explanations are also presented.

Original languageEnglish (US)
Pages (from-to)2348-2356
Number of pages9
JournalBiochemistry
Volume30
Issue number9
StatePublished - 1991
Externally publishedYes

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Immunoglobulins
Ligands
Immunoglobulin E
Haptens
Kinetics
Binding Sites
Fluorescein
Rate constants
Agglomeration

ASJC Scopus subject areas

  • Biochemistry

Cite this

Dissociation kinetics of bivalent ligand-immunoglobulin e aggregates in solution. / Posner, Richard G.

In: Biochemistry, Vol. 30, No. 9, 1991, p. 2348-2356.

Research output: Contribution to journalArticle

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