Binding of bacterial lipopolysaccharide to histocompatibility-2-complex proteins of mouse lymphocytes.
The membrane binding sites for lipopolysaccharide (LPS) were isolated by affinity chromatography of the solubilized membranes prepared from 125I-labeled mouse B-cells and T-cells on an affinity adsorbent prepared by coupling Salmonella minnesota R595 LPS to activated Sepharose 4B. The membrane proteins bound to the affinity adsorbent and eluted with 1.0% Triton X-100 were analyzed according to their mobility on polyacrylamide gel electrophoresis in sodium dodecylsulphate. These membrane proteins were further identified by immunoprecipitation with specific antisera. Immunoglobulins, possibly immunoglobulins M and D, were identified in the eluate from the B-cell membranes. The histocompatibility-2-complex proteins (H-2D, H-2K and Ia antigens) were also found to be binding sites for LPS on both B-cells and T-cells.
D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology; D002458:Cell Fractionation; D002462:Cell Membrane / Q000276:immunology / Q000648:ultrastructure; D006649:Histocompatibility Antigens; D008070:Lipopolysaccharides; D008214:Lymphocytes / Q000276:immunology* / Q000648:ultrastructure; D051379:Mice; D011233:Precipitin Tests; D011485:Protein Binding; D013601:T-Lymphocytes / Q000276:immunology
D006649:Histocompatibility Antigens; D008070:Lipopolysaccharides