Hepatitis B antigen: antigenic sites related to human serum proteins revealed by affinity chromatography.
Hepatitis B antigen-associated particles, isolated from sera of antigen carriers, were submitted to affinity chromatography on columns of insolubilized antibodies to normal human plasma. The particles adsorbed to the immunosorbent at pH 7.2 and were subsequently eluted at pH 2.2. Exposure of the particles to 8 M urea, 5 M KI, pH 2.2, detergents, organic solvents, or proteolytic enzymes failed to prevent their subsequent adsorption to the immunosorbent. This suggests that antigenic determinants related to human plasma proteins are constituent components of hepatitis B antigen-associated particles. These determinants are distinct from the group-specific (a) and subtype-specific (d or y) sites of the hepatitis B antigen and appear to be related to antigenic specificities on prealbumin, albumin, apolipoproteins C and D, and the gamma-chain of immunoglobulin G.
D000818:Animals; D001666:Binding Sites, Antibody; D001798:Blood Proteins; D002846:Chromatography, Affinity; D003902:Detergents / Q000494:pharmacology; D000939:Epitopes; D006511:Hepatitis B Antigens; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000494:pharmacology; D011193:Potassium Iodide / Q000494:pharmacology; D012756:Sheep / Q000276:immunology; D014508:Urea / Q000494:pharmacology
D001798:Blood Proteins; D003902:Detergents; D000939:Epitopes; D006511:Hepatitis B Antigens; D011193:Potassium Iodide; D014508:Urea; D010447:Peptide Hydrolases