Immunochemical Study of Hemoglobin-Free Human Erythrocyte Membranes

[摘要] The plasma membrane of human erythrocytes has been characterized as an antigenic entity distinct from cytoplasmic components, certain of which may be included in hemoglobin-free ghosts prepared by hypotonic lysis of erythrocytes at pH 7.4. Lyophilization and subsequent rehydration resulted in the partition of the protein in hemoglobin-free membranes between a major, insoluble fraction from which pure erythrocyte mucoid (virus receptor substance, VRS) was extractable, and a minor, soluble fraction (soluble ghost protein, SGP). The SGP fraction, free of detectable receptor activity, comprised at least four proteins, one of which cross-reacted with VRS. The latter, in quantitative precipitin, double diffusion, electrophoretic and immunoelectrophoretic analyses, behaved as a single antigen. Together with components of SGP, VRS was held responsible for the “nonspecific” agglutinins provoked in rabbits by the injection of whole erythrocytes, hemolyzates or fractions containing plasma membrane constituents. SGP components were therefore assumed to be exposed at the surface of intact erythrocytes in intimate association with mucoid which bears blood group antigens and virus receptors. The solubilization of erythrocyte membranes by means of detergents and organic solvents results in the partition of lipid, protein and polysaccharide in a manner distinctly different from that which follows lyophilization and rehydration as described in this report.

[学科分类] 生物科学（综合）