Comparative chemical analyses of the alloantigenic fragments of HL-A antigens.
Papain-solubilized HL-A antigens have been shown to contain two polypeptide fragments: beta2-micro-globulin with a molecular weight of approximately 12,000 and a larger fragment with a molecular weight of about 34,000. The large fragments isolated from two HL-A preparations carrying different specificities appeared homogeneous both by immunoelectrophoresis and sodium dodecyl sulfate-acrylamide electrophoresis. Both HL-A antigen preparations contained the same NH2-terminal (glycine) and the same COOH-terminal residue (serine). The carbohydrate content of the large fragment was 12.9%, making the carbohydrate-free molecular weight approximately 30,000. Small but significant differences have been found in the amino acid compositions and tryptic peptide maps of the two large fragments containing different specificities.
D000596:Amino Acids / Q000032:analysis; D002460:Cell Line; D055598:Chemical Phenomena; D002621:Chemistry; D005690:Galactose / Q000032:analysis; D005944:Glucosamine / Q000032:analysis; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D006801:Humans; D006868:Hydrolysis; D007122:Immunoelectrophoresis; D008358:Mannose / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D012794:Sialic Acids / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D010446:Peptide Fragments; D012794:Sialic Acids; D014357:Trypsin; D005944:Glucosamine; D008358:Mannose; D005690:Galactose