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Biochemical evidence for a separate,MHC-linked locus encoding H-2.28 antigens

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Abstract

In comparing the tryptic peptide maps of the H-2L and H-2D glycoprotein antigens isolated from NP-40 lysates of RADA1 (H-2 a) leukemic cells, no more than 37% of the observed arginine-containing tryptic peptides are found to be homologous. Thus, the primary amino-acid sequences of these two antigens are probably less than 90% homologous. This constitutes the strongest evidence to date that the MHC-linkedH-2L region encodes H-2L antigens separately from theH-2D region, even though H-2L antigens bear D-end-associated antigenic determinants of the H-2.28 family. The anti-H-2.28 alloantiserum (k×r anti h2) used to precipitate H-2L antigens in this investigation was the NIH contract antiserum D28b. As the tryptic peptide maps also surprisingly revealed, D28b precipitates H-2D antigens as well and, thus, anti-H-2.4 immunoadsorbants were employed to isolate H-2L free of H-2D antigens. In light of the dual specificity of D28b, its reactivity with BALB/c-H-2 dm2 mutant cells was re-examined. Even though mutant lymphocytes, which lack H-2L but not H-2D antigens, are not cytotoxically lysed by D28b (as are parental H-2d cells), D28b appears to precipitate H-2D antigens from NP-40 extracts of mutant splenocytes.

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  1. Department of Biological Sciences, University of California at Santa Barbara, 93106, Santa Barbara, California

    Duane W. Sears & Catherine M. Polizzi

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  1. Duane W. Sears
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  2. Catherine M. Polizzi
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Sears, D.W., Polizzi, C.M. Biochemical evidence for a separate,MHC-linked locus encoding H-2.28 antigens. Immunogenetics 10, 67–82 (1980). https://doi.org/10.1007/BF01561553

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