Immunological and chemical purity of papain-solubilized HL-A antigens.
Three preparations of purified papain-solublized HL-A antigens have been radiolabeled by reductive methylation using formaldehyde and potassium boro[3H]hydride, and their reaction with specific HL-A antisera has been investigated. Greater than 99 percent of the radioactivity in the [3H]HL-A2 preparation could be complexed with several HL-A2 antisera, but not with specificity controls. The other two preparations, which contained mixtures of HL-A antigenic specificities (HL-A7,12 an HL-A3,W25;12,27), showed 63 per cent and 70 per cent complex formation with mixtures of the appropriate HL-A antisera. The N-terminal amino acid of both subunits has been determined for the three HL-A antigen preparations. In all cases the only detectable N-terminal amino acids were isoleucine for the small subunits, beta-2-microblogulin, and glycine for the larger subunit.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000918:Antibody Specificity; D000937:Antigen-Antibody Reactions; D002460:Cell Line; D002850:Chromatography, Gel; D003619:Dansyl Compounds; D004591:Electrophoresis, Polyacrylamide Gel; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D006801:Humans; D010206:Papain; D010446:Peptide Fragments / Q000032:analysis; D014316:Tritium
D000596:Amino Acids; D003619:Dansyl Compounds; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D010446:Peptide Fragments; D014316:Tritium; D010206:Papain