Purification of HLA-linked B lymphocyte alloantigens in immunologically active form by preparative sodium dodecyl sulfate-gel electrophoresis and studies on their subunit association.
The HLA-linked B cell alloantigen (p29,34) is composed of two subunits of 29,000 (p29) and 34,000 (p34) molecular weight. The partially purified HLA-linked B cell alloantigen was purified by a final step of preparative sodium dodecyl sulfate-gel electrophoresis. An antiserum was prepared against p29,34 which specifically lysed B lymphocytes. In sodium dodecyl sulfate at 21 degrees, p29 and p34 remained noncovalently associated and retained immunologic activity; subunit dissociation at higher temperatures correlated with loss of immunologic activity. Although the pI values of p29 and p34 are 6.1 and 5.2, respectively, the subunits co-electrofocus under nondenaturing conditions. In addition, cross-linking studies showed the B cell antigen has a (p29)1(p34)1 subunit structure.
D000937:Antigen-Antibody Reactions; D001402:B-Lymphocytes / Q000276:immunology*; D002460:Cell Line; D002478:Cells, Cultured; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D006358:Hot Temperature; D006801:Humans; D007519:Isoantigens / Q000302:isolation & purification; D046911:Macromolecular Substances; D008970:Molecular Weight; D013601:T-Lymphocytes / Q000276:immunology; D014508:Urea
D006680:HLA Antigens; D006649:Histocompatibility Antigens; D007519:Isoantigens; D046911:Macromolecular Substances; D014508:Urea