Wiman K, Larhammar D, Claesson L, Gustafsson K, Schenning L, Bill P, Böhme J, Denaro M, Dobberstein B, Hammerling U, Kvist S, Servenius B, Sundelin J, Peterson P A, Rask L
Proc Natl Acad Sci U S A. 1982 Mar;79(6):1703-7. doi: 10.1073/pnas.79.6.1703.
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.
主要组织相容性复合体中的HLA - D位点控制着遗传多态性HLA - DR抗原的表达。编码这些抗原β链的mRNA是从人淋巴母细胞系Raji中部分纯化得到的。该mRNA被转录成双链cDNA并克隆到大肠杆菌中。通过杂交筛选获得的一个克隆pDR - β - 1,携带一个1070个碱基对的插入片段,该片段包含除信号序列外的所有编码区以及大部分非翻译区。为了鉴定pDR - β - 1,对来自Raji细胞的高度纯化的HLA - DR抗原β链进行了氨基末端氨基酸序列测定。该序列与从pDR - β - 1编码区5'端核苷酸序列推导出来的序列显示出广泛的同源性。综合来看,氨基酸和核苷酸序列有力地表明Raji细胞至少含有两个β链基因座。