The immunologic and molecular profiles of HLA antigens isolated from urine.
Human urine was shown to be a good source for the isolation of immunologically functional HLA-A9 antigens. The use of complex solubilization procedures can be avoided since the antigens are present in soluble form and are not complexes with membrane fragements. Purification in excess of 400-fold could be achieved by the application of cellulose ion exchange chromatography, isoelectric focusing, and acrylamide gel electrophoresis. The purified HLA-A9 antigen is composed of a glycoprotein of m.w. 38,000 and beta2-microglobulin, a peptide of m.w. 12,000. HLA-A9 antigens isolated from urine proved to be immunologically functional since they not only reacted specifically with anti-HLA-A9 alloantibody but also elicited anti-HLA-A9 xenoantibodies. These antibodies when covalently attached to Sepharose 4B specifically bound HLA-A9 antigens isolated from both serum and urine.
D001120:Arginine / Q000494:pharmacology; D000939:Epitopes; D006680:HLA Antigens / Q000302:isolation & purification / Q000652:urine*; D006649:Histocompatibility Antigens / Q000652:urine*; D006801:Humans; D008074:Lipoproteins; D008970:Molecular Weight; D001613:beta 2-Microglobulin / Q000652:urine
D000939:Epitopes; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D008074:Lipoproteins; D001613:beta 2-Microglobulin; D001120:Arginine