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

Larry R Pease, Bruce M. Ewenstein, Diane McGovern, Roger W. Melvold, Tosiki Nisizawa, Stanley G. Nathenso

Research output: Contribution to journalArticle

9 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)7-17
Number of pages11
JournalImmunogenetics
Volume17
Issue number1
DOIs
StatePublished - Jan 1983
Externally publishedYes

ASJC Scopus subject areas

  • Immunology
  • Genetics

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    Pease, L. R., Ewenstein, B. M., McGovern, D., Melvold, R. W., Nisizawa, T., & Nathenso, S. G. (1983). Biochemical studies on the H-2K mutant B6.C-H-2bm10 Immunogenetics, 17(1), 7-17. https://doi.org/10.1007/BF00364285