Devos R, Vandekerckhove J, Rolink A, Plaetinck G, Van der Heyden J, Fiers W, Tavernier J
Roche Research Gent, Belgium.
Eur J Immunol. 1991 May;21(5):1315-7. doi: 10.1002/eji.1830210533.
A polypeptide chain for the mouse interleukin 5 receptor (IL5R) was purified from detergent-lysed B13 cells, a mouse IL5-dependent pre-B cell line. Purification was by a single immunoaffinity chromatographic step using an anti-mouse IL5R monoclonal antibody, R52. Internal amino acid sequence was obtained from four trypsin-generated peptides. All peptides were found to be present in the published amino acid sequence of a mouse IL3R and the mouse IL3R-like protein deduced from the cDNA. This indicates that the mouse IL5R and the mouse IL3R have a homologous polypeptide in common and suggests that the specificity of these lymphokine receptors is mainly generated by association with another ligand-specific polypeptide chain.
从小鼠白细胞介素5受体（IL5R）的一条多肽链是从用去污剂裂解的B13细胞（一种依赖小鼠IL5的前B细胞系）中纯化得到的。纯化过程通过使用抗小鼠IL5R单克隆抗体R52的单一免疫亲和色谱步骤进行。从四种胰蛋白酶产生的肽段中获得了内部氨基酸序列。发现所有肽段都存在于已发表的小鼠IL3R氨基酸序列以及从cDNA推导的小鼠IL3R样蛋白中。这表明小鼠IL5R和小鼠IL3R有一条共同的同源多肽链，并且提示这些淋巴因子受体的特异性主要是通过与另一条配体特异性多肽链结合产生的。
