Biochemical comparison of the T6 antigen and HLA-A,B antigens.
The human thymic differentiation antigen T6, which was found to be associated with beta 2-microglobulin, was compared to the HLA-A,B antigens. Using a heteroantiserum prepared against denatured heavy chains of HLA-A,B antigens, no cross-reactivity with denatured T6 could be detected. The molecular weight of the protein backbone of T6 was found to be 34,000 as compared to 40,000 for the HLA-A,B antigens. Also, not only was the percentage of carbohydrate of T6 (25-35%) different from the HLA-A,B antigens (10%), but lectin binding studies showed that their sugar composition may differ. The two forms of T6, which previously had been found on MOLT-4 cells, appeared to have different levels of glycosylation, but apparently had the same protein backbone. T6, like HLA, has a hydrophobic domain, since it could be labeled with [125I]iodonaphthylazide. We conclude from these studies that T6 may be a class I MHC antigen which is different from the classical HLA-A,B antigens.
D000945:Antigens, Differentiation, T-Lymphocyte; D000954:Antigens, Surface / Q000032:analysis*; D003429:Cross Reactions; D000939:Epitopes; D006023:Glycoproteins / Q000276:immunology; D006680:HLA Antigens / Q000032:analysis*; D006801:Humans; D008970:Molecular Weight; D009844:Oligosaccharides / Q000032:analysis; D013601:T-Lymphocytes / Q000276:immunology*; D001613:beta 2-Microglobulin / Q000032:analysis
D000945:Antigens, Differentiation, T-Lymphocyte; D000954:Antigens, Surface; D000939:Epitopes; D006023:Glycoproteins; D006680:HLA Antigens; D009844:Oligosaccharides; D001613:beta 2-Microglobulin