TY - JOUR
T1 - Solubilization and characterization of a low-affinity histamine-binding site on human blood mononuclear cells
AU - Warlow, Robert S.
AU - White, Robert
AU - Bernard, Claude C.A.
PY - 1986
Y1 - 1986
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0022578917&partnerID=8YFLogxK
U2 - 10.1016/0161-5890(86)90137-9
DO - 10.1016/0161-5890(86)90137-9
M3 - Article
C2 - 3088433
AN - SCOPUS:0022578917
VL - 23
SP - 393
EP - 402
JO - Molecular Immunology
JF - Molecular Immunology
SN - 0161-5890
IS - 4
ER -