Purification of HLA antigens from urine.
HLA antigens were purified from urines of kidney transplanted patients, HLA was recovered as a single peak of 45,000 mol wt that was dissociated into beta2-microglobulin and a 33,000 mol wt fraction bearing the allospecificity. The purified fractions contain carbohydrates but no lipids. Electrophoretical mobility and the relative salt concentration of eluting buffers in DEAE-Sephadex chromatography were determined for six antigens of the A locus and seven antigens of the B locus. Isolectric points of antigens A1, A2, A9, and B12 were measured. Physiochemical characteristics of HLA purified from urine appear to be similar to those of papain-solubilized cell membrane HLA. Urinary HLA was shown to originate from serum and not from renal or ureteric tissue.
D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003601:Cytotoxicity Tests, Immunologic; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D006680:HLA Antigens / Q000032:analysis / Q000302:isolation & purification* / Q000652:urine; D006649:Histocompatibility Antigens / Q000302:isolation & purification*; D006801:Humans; D007526:Isoelectric Point; D016030:Kidney Transplantation; D014184:Transplantation, Homologous
D000939:Epitopes; D006680:HLA Antigens; D006649:Histocompatibility Antigens