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
Immunogeneticsjournal_title
Immunogeneticsauthors
Pease LR,Ewenstein BM,McGovern D,Melvold RW,Nisizawa T,Nathenson SGdoi
10.1007/BF00364285subject
Has Abstractpub_date
1983-01-01 00:00:00pages
7-17issue
1eissn
0093-7711issn
1432-1211journal_volume
17pub_type
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