Rémy J J, Salamero J, Charreire J
Acta Endocrinol Suppl (Copenh). 1987;281:186-92. doi: 10.1530/acta.0.114s186.
Purification of the thyrotropin (TSH) binding sites from cloned human thyroid cells (GEJ) was performed after biosynthetic labelling of the cells, affinity chromatography on a human TSH-sepharose column and polyacrylamide gel electrophoresis in sodium dodecyl sulphate (PAGE-SDS). The relative molecular mass (Mr) of the GEJ cell TSH receptor (TSH-R) was approximately 48,000. This was confirmed by cross-linking [125I]TSH to GEJ binding sites with two homobifunctional agents: dimethyl suberimidate and disuccinimidyl suberate. Moreover, the absence of a dithiothreitol effect demonstrated that the TSH binding site on GEJ cells is formed by a single chain lacking disulphide bonds.
对克隆的人甲状腺细胞（GEJ）进行生物合成标记后，通过在人促甲状腺激素-琼脂糖柱上进行亲和层析以及在十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE），从这些细胞中纯化促甲状腺激素（TSH）结合位点。GEJ细胞促甲状腺激素受体（TSH-R）的相对分子质量（Mr）约为48,000。用两种同双功能试剂：亚胺基二琥珀酸二甲酯和辛二酸二琥珀酰亚胺酯将[125I]TSH交联到GEJ结合位点，证实了这一点。此外，二硫苏糖醇无作用表明GEJ细胞上的TSH结合位点由一条不含二硫键的单链构成。
