N-terminal and cDNA characterization of murine lymphocyte antigen Ly-6C.2
| Autor: | R G Palfree, S Sirlin, F J Dumont, U Hämmerling |
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| Rok vydání: | 1988 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 140:305-310 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.140.1.305 |
| Popis: | The Ly-6C.2 molecule was purified from K36 tumor cells by affinity chromatography and gel filtration. The electrophoretically homogeneous preparation, with m.w. 15,000, was tested with a panel of antibodies that confirmed the presence of the LY-6C.2 epitope. An N-terminal sequence of 39 amino acids was obtained showing 59% homology with the corresponding portion of the Ly-6A.2 polypeptide. Based on the least homologous (29%) 14 amino acid segment, an oligonucleotide probe was constructed, and Ly-6C.2 cDNA was cloned from a BW5147 cDNA library. A 794-base pair cDNA containing the entire coding region had 82% homology with Ly-6A.2 cDNA. The encoded polypeptide sequence of 131 amino acids containing a perfect correlation with the N-terminal sequence data was 63% homologous with that of Ly-6A.2. The greatest homology was in the leader, first 16 N-terminal and last 39 C-terminal amino acids. The latter are likely to be important in determining the attachment of glycophosphatidylinositol. Despite results indicating fewer disulfide constraints in the Ly-6C molecule, the predicted sequence contains 10 cysteine residues nearly perfectly matched with those predicted in Ly-6A. |
| Databáze: | OpenAIRE |
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