Affinity chromatography of beta2-microglobulin from human lymphocytes on concanavalin-A-sepharose. Determination of carbohydrate-containing protein molecules complexed with beta2-microglobulin.
Beta2-microglobulin was extracted from human lymphocytes with nonionic detergent and separated by affinity chromatography on concanavalin-A-Sepharose. The retarded part of beta2-microglobulin is assumed to be associated with HLA antigens. Using a radioimmunoassay for beta2-microglobulin, the average number of presumably free beta2-microglobulin molecules and of presumably HLA-associated beta2-microglobulin molecules per lymphocyte was estimated to be 3.8 x 10(5) and 1.4 x 10(5), respectively.
D001609:Beta-Globulins / Q000032:analysis*; D002846:Chromatography, Affinity; D003208:Concanavalin A; D006680:HLA Antigens; D006801:Humans; D008214:Lymphocytes / Q000032:analysis*; D011485:Protein Binding; D011863:Radioimmunoassay; D012685:Sepharose; D001613:beta 2-Microglobulin / Q000032:analysis*
D001609:Beta-Globulins; D006680:HLA Antigens; D001613:beta 2-Microglobulin; D003208:Concanavalin A; D012685:Sepharose