Further biochemical studies of the human B-cell differentiation antigens B1 and B2.
Two human B lymphocyte-associated antigens, B1 and B2, were studied by immunoprecipitation using monoclonal antibodies. B1 was found to be a nonglycosylated protein of MW 35 kD, phosphorylated at serine and threonine. B2, a 140 kD MW antigen, was characterized as a glycoprotein without phosphorylated sites. Both proteins were found to contain portions which could be labeled with 125I-iodonaphthylazide. The B1 protein displayed hydrophobic properties whereas B2 had a more amphiphilic character.
D000944:Antigens, Differentiation, B-Lymphocyte; D000954:Antigens, Surface / Q000302:isolation & purification; D001402:B-Lymphocytes / Q000276:immunology*; D002460:Cell Line; D006023:Glycoproteins / Q000276:immunology; D006801:Humans; D008565:Membrane Proteins / Q000276:immunology; D008970:Molecular Weight; D010750:Phosphoproteins / Q000276:immunology
D000944:Antigens, Differentiation, B-Lymphocyte; D000954:Antigens, Surface; D006023:Glycoproteins; D008565:Membrane Proteins; D010750:Phosphoproteins