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

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.

journal_name

Immunogenetics

journal_title

Immunogenetics

authors

Pease LR,Ewenstein BM,McGovern D,Melvold RW,Nisizawa T,Nathenson SG

doi

10.1007/BF00364285

subject

Has Abstract

pub_date

1983-01-01 00:00:00

pages

7-17

issue

1

eissn

0093-7711

issn

1432-1211

journal_volume

17

pub_type

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