Differential glycosylation of murine B cell and spleen adherent cell Ia antigens.

Examination of I-A and I-E molecules from purified B cells and splenic adherent cells from various haplotypes revealed a consistent difference in isoelectric focusing (IEF) that has been localized to the alpha-chain. alpa-Chains from B cells appeared heterogeneous and contained acidic IEF bands absent from the adherent cell I-A molecules. No difference in Ia beta-chain or H-2 IEF patterns was observed when B cell and adherent cell preparatios were compared when B cell and adherent cell preparations were compared. I-A alpha-chain preparations from the 2 cell sources showed no differences in 3H-leucine-labeled tryptic peptides separated by reverse-phase high-pressure liquid chromatography. Digestion with neuraminidase, kinetics of labeling, and subcellular distribution indicated that the extra acidic IEF bands in B cell Ia represent a mature, more heavily sialated form of alpha-chain that is not present in adherent cells. The selective differential glycosylation of B cell and adherent cell Ia could have some relation to the function of those cell types or to cell type-specific recognition of those cells.