ANALYSIS OF A SEROLOGICAL DETERMINANT OF H-Y ANTIGEN: EVIDENCE FOR CARBOHYDRATE SPECIFICITY USING AN H-Y SPECIFIC MONOCLONAL ANTIBODY

Using a monoclonal antibody to H-Y antigen we characterized the molecular determinant responsible for H-Y reactivity. H-Y-positive cells were treated with enzymes which alter carbohydrate structure and then were tested for their ability to absorb monoclonal anti-H-Y antibody. Indications are that the serological determinant recognized by this antibody is a glycoconjugate containing terminal non-reducing and internal galactosyl residues.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/74651/1/j.1744-313X.1984.tb01057.x.pd

Partial characterization of Ia antigens from murine lymphoid cells

Congenic anti-Ia antisera were used to bind radiolabelled Ia antigens from cells of various strains of mice of known H-2 haplotype. The results indicate that Ia antigens are proteins of molecular weight 30,000 to 35,000 daltons. The Ia antigens are distinct from known H-2 antigens as judged by independent immunoprecipitation as well as by molecular weight. Ia antigens are synthesized by, and are present on the surface of lymphoid cells as evidenced by incorporation studies using 3 H-leucine and enzymatic radioiodination of cells, respectively. Tissue distribution of cell surface Ia suggests that Ia antigens are on B cells. Ia antigens were detected in the incubation media of 3 H-leucine labeled splenocytes suggesting that antigens may be secreted.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/46728/1/251_2005_Article_BF01564048.pd