Amino acid sequence analysis of the H-2Kk alloantigen: complete sequence of residues 1-98 and partial sequence from 99 to 263.

The H-2Kk molecule was purified by immunoprecipitation from the glycoprotein fraction of Nonidet P-40 extracts of RDM 4 mouse tumor cells. Cyanogen bromide cleavage of the major papain fragment yielded three peptides, the largest of which consisted of three disulfide-linked peptides which could be separated after reduction and alkylation. These peptides were readily aligned by their homology to similar fragments derived from other H-2 class I molecules. Amino acid sequence analyses of the two nondisulfide-linked peptides, peptide E (residues 1-52) and peptide D (53-98), yielded the following NH2-terminal sequence for the H-2Kk molecule: [sequence in text]. Comparison of this sequence with those of other H-2 class I molecules revealed that: (1) Lys-19, Val-55, Glu-56, Asn-63 and Ile-73 are unique to the H-2Kk molecule; and (2) H-2Kk shares 79-83% homology in this region with other mouse class I molecules. Partial NH2-terminal amino acid sequences are also reported for the three disulfide-linked peptides. Several discrepancies from previously reported partial sequences of the H-2Kk molecule were detected.