Primary structure of murine major histocompatibility complex alloantigens: amino acid sequence of the amino-terminal one hundred and seventy-three residues of the H-2Kb glycoprotein

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Abstract
The amino-terminal 173 residues of the murine histocompatibility antigen H-2Kb were assigned by using radiochemical methodology. The complete sequence of an 86 residue glycopeptide (CN-Ib), which is 1 of the 5 major CNBr fragments of Kb, was determined by analysis of peptides obtained from digests using thrombin and V8 staphylococcal protease. Complete sequences were obtained for the three large thrombic peptides; these were aligned by using peptides from the V8 protease digest. Alignment of the CNBr fragments was carried out by using [35S]Met-labeled peptides from a tryptic digest of the papain-cleaved H-2Kb molecule. Positive identification was possible for all the common amino acids except Asp (Asp) which was indirectly assigned and which is designated in italics. The sequence obtained in these studies was described. These data represent the longest reported amino acid sequence determined by utilizing radiochemical methodology and provide the first extensive information on the primary structure of murine histocompatibility antigens.