Abstract |
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.
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Authors | E P Lillehoj, J E Coligan |
Journal | Molecular immunology
(Mol Immunol)
Vol. 21
Issue 3
Pg. 185-90
(Mar 1984)
ISSN: 0161-5890 [Print] England |
PMID | 6717443
(Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Amino Acids
- H-2 Antigens
- H-2K(K) antigen
- Peptide Fragments
- Papain
- Cyanogen Bromide
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Topics |
- Amino Acid Sequence
- Amino Acids
(analysis)
- Animals
- Cyanogen Bromide
- H-2 Antigens
(analysis)
- Mice
- Papain
- Peptide Fragments
(isolation & purification)
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