Taketani S, Krangel M S, Spits H, de Vries J, Strominger J L
J Immunol. 1984 Aug;133(2):816-21.
It has been demonstrated previously that lymphocytes of donor CF (HLA-A29,w33; B7,14) are not recognized by the HLA-B7-specific CTL clone HG-31. This report presents a structural comparison of the HLA-B7 antigen of donor CF with a "normal" HLA-B7 antigen, derived from the cell line JY. Isoelectric focusing showed that CF HLA-B7 heavy chains were more acidic than JY HLA-B7 heavy chains by the equivalent of a single charge. High pressure liquid chromatography and ion exchange chromatography comparisons of double-labeled tryptic peptides revealed a single detectable difference, which corresponded to the tryptic peptide spanning residues 112 to 121 on the HLA-B7 heavy chain. Although the complete amino acid sequence of this peptide was not obtained, the partial sequence indicates a substitution of an unidentified amino acid for tyrosine at position 116 of the heavy chain. This residue is found to vary among HLA specificities and to be altered in many H-2Kb mutants.
先前已证明，供体CF（HLA - A29，w33；B7，14）的淋巴细胞不被HLA - B7特异性CTL克隆HG - 31识别。本报告呈现了供体CF的HLA - B7抗原与源自JY细胞系的“正常”HLA - B7抗原的结构比较。等电聚焦显示，CF HLA - B7重链比JY HLA - B7重链酸性更强，相当于多出一个电荷。对双标记胰蛋白酶肽段进行的高压液相色谱和离子交换色谱比较显示出一个可检测到的差异，该差异对应于HLA - B7重链上跨越第112至121位残基的胰蛋白酶肽段。虽然未获得该肽段的完整氨基酸序列，但部分序列表明重链第116位的酪氨酸被一个未鉴定的氨基酸取代。发现该残基在HLA特异性之间存在差异，并且在许多H - 2Kb突变体中发生了改变。
