Studies of antigen binding on human basophils. I. Antigen binding and functional consequences

Donald Macglashan, L. M. Lichtenstein

Research output: Contribution to journalArticle

Abstract

We developed an assay to study simultaneously antigen binding and its functional consequences on human basophils. Using a 125iodine-labeled penicillin-human serum albumin conjugate, we were able to detect as few as 100 molecules of antigen bound to purified basophils. We found that histamine release could be initiated with fewer than 100 molecules of antigen and that the optimum for histamine release occurred at a concentration at which 10 to 15% of the available antibody-binding sites were occupied. Analysis of the binding kinetics in the presence of monovalent hapten allowed a calculation of the affinity constant for the antibody:hapten association; the value of 2 to 3 x 106/Msec confirmed an earlier independent calculation. Binding data also suggested a 25% fraction of the bound antigen was binding in monogamous bivalent form. It is anticipated that studies of this kind will delineate the nature of the antibody-antigen reaction on cell surfaces.

Original languageEnglish (US)
Pages (from-to)2330-2336
Number of pages7
JournalJournal of Immunology
Volume130
Issue number5
StatePublished - 1983

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Basophils
Antigens
Haptens
Histamine Release
Antigen-Antibody Reactions
Antibody Binding Sites
Antibody Affinity
Serum Albumin
Penicillins
I-antigen

ASJC Scopus subject areas

  • Immunology

Cite this

Studies of antigen binding on human basophils. I. Antigen binding and functional consequences. / Macglashan, Donald; Lichtenstein, L. M.

In: Journal of Immunology, Vol. 130, No. 5, 1983, p. 2330-2336.

Research output: Contribution to journalArticle

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