The detection and partial characterization of the major histocompatibility antigens encoded by the three H-2 loci, K, D, and L were performed by analyzing immunoprecipitates from detergent-solubilized radiolabeled cells on two-dimensional gels. Each locus was found to code for a population of proteins heterogeneous in both charge and m.w. Only part of the heterogeneity was shown to be due to sialylation as demonstrated by shifts in mobility after neuraminidase treatment of antigen preparations. The 2-D gel analysis of the H-2K, H-2D, and H-2L antigens of the d haplotype shows that each constitutes a distinct series of products.
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