Test of a theory relating to the cross-linking of IgE antibody on the surface of human basophils
Journal Article
·
· J. Immunol.; (United States)
OSTI ID:5806630
Recent mathematical models of bivalent hapten-induced histamine release from basophils predict that under appropriate conditions histamine release is maximum when cross-link formation is maximum, at a hapten concentration equal to 1/(2K/sub a/), where K/sub a/ is the average affinity constant of the hapten for a single IgE binding site. To test this prediction the authors sensitized human basophils with a monoclonal anti-dinitrophenol IgE and generated histamine release dose-response curves with a bivalent hapten, ..cap alpha..,epsilon-DNP-lysine. The monoclonal IgE has a published affinity constant of 7.1 x 10/sup 7/ M/sup -1/ for epsilon-DNP-lysine as determined by equilibrium dialysis. From the position of the maximum of the histamine dose-response curves, both in the presence and in the absence of monovalent DNP hapten, the authors determine that the sensitizing IgE has an intrinsic affinity constant of 6.9 +/- 0.5 x 10/sup 7/ M/sup -1/ for such that-DNP-lysine and 1.2 +/- 0.6 x 10/sup 6/ M/sup -1/ for ..cap alpha..-DNP-lysine. The agreement between the two estimates of the epsilon-DNP-lysine affinity constant, one from histamine release experiments involving surface bound IgE and one from binding experiments involving IgE free in solution, 1) is consistent with a central prediction of the theory of cross-linking and 2) indicates that the hapten-binding properties of the IgE are unaffected by its being bound to Fc/sub epsilon/ receptors on the basophil surface. 30 references, 3 figures, 3 tables.
- Research Organization:
- Johns Hopkins Univ., Baltimore, MD
- OSTI ID:
- 5806630
- Journal Information:
- J. Immunol.; (United States), Journal Name: J. Immunol.; (United States) Vol. 135:6; ISSN JOIMA
- Country of Publication:
- United States
- Language:
- English
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Journal Article
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Sat Jul 01 00:00:00 EDT 1978
· J. Immunol.; (United States)
·
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Theory of equilibrium binding of asymmetric bivalent haptens to cell surface antibody: application to histamine release from basophils
Journal Article
·
Tue Aug 01 00:00:00 EDT 1978
· J. Immunol.; (United States)
·
OSTI ID:7053433
Histamine release due to bivalent penicilloyl haptens: the relation of activation and desensitization of basophils to dynamic aspects of ligand binding to cell surface antibody
Journal Article
·
Wed Jan 31 23:00:00 EST 1979
· J. Immunol.; (United States)
·
OSTI ID:6394393
Related Subjects
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AFFINITY
AMINES
AMINO ACIDS
ANIMALS
ANTIBODIES
AZOLES
BASOPHILS
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CROSS-LINKING
DATA
DOSE-RESPONSE RELATIONSHIPS
EXPERIMENTAL DATA
GLOBULINS
HETEROCYCLIC COMPOUNDS
HISTAMINE
IMIDAZOLES
IMMUNOGLOBULINS
INFORMATION
KINETICS
LEUKOCYTES
LYSINE
MAMMALS
MAN
MATERIALS
MATHEMATICAL MODELS
MEMBRANE PROTEINS
MONOCLONAL ANTIBODIES
NUMERICAL DATA
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
POLYMERIZATION
PRIMATES
PROTEINS
REACTION KINETICS
RECEPTORS
SECRETION
VALENCE
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
AFFINITY
AMINES
AMINO ACIDS
ANIMALS
ANTIBODIES
AZOLES
BASOPHILS
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CROSS-LINKING
DATA
DOSE-RESPONSE RELATIONSHIPS
EXPERIMENTAL DATA
GLOBULINS
HETEROCYCLIC COMPOUNDS
HISTAMINE
IMIDAZOLES
IMMUNOGLOBULINS
INFORMATION
KINETICS
LEUKOCYTES
LYSINE
MAMMALS
MAN
MATERIALS
MATHEMATICAL MODELS
MEMBRANE PROTEINS
MONOCLONAL ANTIBODIES
NUMERICAL DATA
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
POLYMERIZATION
PRIMATES
PROTEINS
REACTION KINETICS
RECEPTORS
SECRETION
VALENCE
VERTEBRATES