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. 1982 Mar;79(6):1703–1707. doi: 10.1073/pnas.79.6.1703

Isolation and identification of a cDNA clone corresponding to an HLA-DR antigen beta chain.

K Wiman, D Larhammar, L Claesson, K Gustafsson, L Schenning, P Bill, J Böhme, M Denaro, B Dobberstein, U Hammerling, S Kvist, B Servenius, J Sundelin, P A Peterson, L Rask
PMCID: PMC346048  PMID: 6952222

Abstract

The HLA-D locus in the major histocompatibility complex controls the expression of the genetically polymorphic HLA-DR antigens. mRNA coding for the beta chains of these antigens was partially purified from the human lymphoblastoid cell line Raji. The mRNA was copied into double-stranded cDNA and cloned in Escherichia coli. One clone, pDR-beta-1, obtained by hybrid selection, carries a 1070-base-pair insert comprising all of the coding region except the signal sequence and a substantial portion of the untranslated region. To identify pDR-beta-1, highly purified HLA-DR antigen beta chains derived from Raji cells were subjected to NH2-terminal amino acid sequence determination. This sequence displayed extensive homology with that deduced from the nucleotide sequence at the 5' end of the pDR-beta-1 coding region. Taken together, the amino acid and nucleotide sequences strongly argue in favor of Raji cells containing at least two beta-chain loci.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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