Properties of the M antigen solubilized from genetically high potassium sheep red cells.
The M antigen genetically associated with the high potassium (HK) status of sheep red cells was solubilized in 0.5% Triton X-100. This procedure did not impair M-antibody binding in the presence of detergent because solubilized membranes bound M-antibody in units equivalent to control membranes. As judged by M-antibody binding, the antigen was found to be stable in 0.5% Triton X-100 at 4 degree C but lost its activity rapidly at 37 degree C or when diluted to low detergent concentrations. However, the formation of the M antigen-antibody complex prior to dilution or exposure to elevated temperature protected the M antigen from inactivation. Brief exposure to alkaline pH released the extrinsic membrane proteins from red cell membranes without solubilizing the M antigen. The intrinsic membrane proteins were further separated by ion exchange chromatography on Affi-Gel 102. M antigenic activity copurified with the sheep specific protein band 2.2 band 6, and the glycoproteins and appeared to be separate from the main portion of band 3 protein.
D000818:Animals; D000936:Antigen-Antibody Complex; D000941:Antigens / Q000302:isolation & purification*; D003902:Detergents; D004355:Drug Stability; D004910:Erythrocyte Membrane / Q000276:immunology* / Q000378:metabolism; D004912:Erythrocytes / Q000276:immunology*; D006461:Hemolysis; D017830:Octoxynol; D011092:Polyethylene Glycols; D011188:Potassium / Q000097:blood*; D012756:Sheep; D012995:Solubility
D000936:Antigen-Antibody Complex; D000941:Antigens; D003902:Detergents; D011092:Polyethylene Glycols; D017830:Octoxynol; D011188:Potassium