Solubilization and characterization of a low-affinity histamine-binding site on human blood mononuclear cells

Robert S. Warlow, Robert White, Claude C.A. Bernard

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10 Citations (Scopus)


The extract of human peripheral blood lymphocytes and monocytes treated with Triton X-100, in direct- and competitive-binding studies, with 10-6-10-2 M [14C]histamine contained a low-affinity binding site whose dissociation constant (Kd 1.8 × 10-4 M) was commensurate with the concns of histamine (10-6-10-3 M) that result from mast cell and basophil degranulation. Binding was enhanced by millimolar concns of divalent cations and by raising the incubation temp from 4 to 37°C. It was inhibited by trypsin, EDTA, agents interacting with thiol groups, and by Triton X-100 concns greater than 0.2%. Thus a low-affinity histamine receptor that maintains its ligand-binding properties after solubilization from the cell surface was identified.

Original languageEnglish
Pages (from-to)393-402
Number of pages10
JournalMolecular Immunology
Issue number4
Publication statusPublished - 1986
Externally publishedYes

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