Submit and disulfide structure of monomeric and dimeric forms of detergent-soluble HLA antigens.
The structure of monomeric and disulfide-bonded dimeric forms of HLA antigens has been studied. Detergent-soluble HLA antigen heavy chains contain one or two easily reduced sulfhydryl groups not found in papain-solubilized HLA antigens, as demonstrated by amino acid analysis (Springer, T. A., and Strominger, J.L. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 2481-2485, and Terhorst, C., Parham, P., Mann, D.L., and Strominger, J.L. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 910-914) and by labeling with iodo[3H]acetate. Dimer formation occurred during purification, since it was prevented by pretreatment of membranes containing HLA antigen with iodoacetamide. Cross-linking studies showed that the non-disulfide-bonded form of HLA antigens contains one subunit each of the Mr = 44,000 heavy chain and the Mr = 12,000 light chain (beta2-microglobulin).
D002250:Carbon Radioisotopes; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003553:Cystine / Q000032:analysis; D003902:Detergents; D004220:Disulfides / Q000032:analysis*; D004586:Electrophoresis; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D007460:Iodoacetamide; D007553:Isotope Labeling; D012995:Solubility; D013438:Sulfhydryl Compounds / Q000032:analysis; D014316:Tritium
D002250:Carbon Radioisotopes; D003902:Detergents; D004220:Disulfides; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D013438:Sulfhydryl Compounds; D014316:Tritium; D003553:Cystine; D007460:Iodoacetamide