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Biochemical studies on the H-2K mutant B6.C-H-2 bm10

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Abstract

The H-2K glycoprotein from the MHC mutant bm10 was analyzed biochemically to determine where primary structural differences distinguished it from the parental standard molecule, Kb. Comparative peptide maps showed differences in two peptides known to be part of the parental CNBr fragment spanning amino acids 139 to 228. Partial sequence analyses of CNBr fragments and tryptic peptides identified two tightly clustered amino acid substitutions at amino acids 165 (Val to Met) and 173 (Lys to unknown). The substitutions in bm10 represent the most carboxy-terminal substitutions characterized in the Kb molecules of the spontaneous, histogenically active H-2 mutants.

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Authors and Affiliations

  1. Department of Microbiology and Immunology and Department of Cell Biology, Albert Einstein College of Medicine, 10461, Bronx, New York

    Larry R. Pease, Bruce M. Ewenstein, Diane McGovern & Stanley G. Nathenso

  2. Northwestern University Medical School Cancer Center, 710 N. Fairbanks Court, 60611, Chicago, Illinois

    Roger W. Melvold

  3. National Institute of Health, Shinagawa-ku, Tokyo, Japan

    Tosiki Nisizawa

Authors
  1. Larry R. Pease
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  2. Bruce M. Ewenstein
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  3. Diane McGovern
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  4. Roger W. Melvold
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  5. Tosiki Nisizawa
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  6. Stanley G. Nathenso
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Pease, L.R., Ewenstein, B.M., McGovern, D. et al. Biochemical studies on the H-2K mutant B6.C-H-2 bm10 . Immunogenetics 17, 7–17 (1983). https://doi.org/10.1007/BF00364285

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  • DOI: https://doi.org/10.1007/BF00364285

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