Nikaido T, Shimizu A, Ishida N, Sabe H, Teshigawara K, Maeda M, Uchiyama T, Yodoi J, Honjo T
Nature. 1984;311(5987):631-5. doi: 10.1038/311631a0.
The human interleukin-2 (IL-2) receptor was purified by affinity chromatography using the anti-Tac monoclonal antibody, and its N-terminal amino acid sequence was determined. Complementary DNA clones were isolated and sequenced to reveal the primary structure of the IL-2 receptor precursor, which has 272 amino acid residues. The receptor is separated into two domains by a putative 19-residue transmembrane region. Two mRNAs (1.4 and 3.5 kilobases) hybridizing to the cDNA clone were found in human T cells bearing the IL-2 receptor. The cDNA directed synthesis of the IL-2 receptor in COS cells.
利用抗 Tac 单克隆抗体通过亲和层析法纯化了人白细胞介素 -2（IL-2）受体，并测定了其 N 端氨基酸序列。分离并测序了互补 DNA 克隆，以揭示 IL-2 受体前体的一级结构，该前体含有 272 个氨基酸残基。受体通过一个推定的 19 个残基的跨膜区域被分为两个结构域。在携带 IL-2 受体的人 T 细胞中发现了与 cDNA 克隆杂交的两种 mRNA（1.4 和 3.5 千碱基）。该 cDNA 指导了 COS 细胞中 IL-2 受体的合成。
