H-2b bound to egg lecithin liposomes: biochemical and functional properties.
Purified H-2b and H-2a molecules were bound to egg lecithin liposomes by a detergent dialysis procedure. Analysis of the liposomes indicated that only 30-50% of bound H-2b is oriented with the hydrophilic, antigenic portion of the molecule toward the outside of the liposome. Saturation of the liposomes occurred at a ratio of 64 molecules of egg lecithin per molecule of H-2b. Liposomes containing H-2 molecules were capable of stimulating spleen cells from primed donors to produce specific, alloreactive, cytotoxic T lymphocytes in vitro. Stimulation was dependent on adherent cells present in the responder spleen cells. Optimal stimulation occurred with highly saturated liposomes and at a ratio of 4-8 micrograms of H-2b per 8 X 10(6) responder cells.
D000818:Animals; D002499:Centrifugation, Density Gradient; D003602:Cytotoxicity, Immunologic; D004591:Electrophoresis, Polyacrylamide Gel; D006183:H-2 Antigens / Q000276:immunology; D008081:Liposomes / Q000276:immunology; D008213:Lymphocyte Activation; D051379:Mice; D008968:Molecular Conformation; D010206:Papain; D010713:Phosphatidylcholines / Q000276:immunology; D013154:Spleen / Q000276:immunology
D006183:H-2 Antigens; D008081:Liposomes; D010713:Phosphatidylcholines; D010206:Papain