Møldrup A
Hagedorn Research Laboratory, Gentofte, Denmark.
Exp Clin Endocrinol. 1989 May;93(2-3):286-92. doi: 10.1055/s-0029-1210870.
Growth hormone receptors from a rat insulinoma cell line, RIN-5AH were solubilized in the non-ionic detergent Triton X-100. A radioreceptor assay based on polyethylene glycol precipitation of the growth hormone: receptor complex showed time-dependent and saturable hormone binding. The affinity in detergent solution for biosynthetic human growth hormone of approx. 6 ng/ml was found similar to that of intact RIN cells. The solubilization and receptor assay conditions described are useful for further characterization and purification of RIN cell growth hormone receptors, which might provide an initial insight into the molecular mechanism of the growth hormone effects on islet beta-cells.
来自大鼠胰岛素瘤细胞系RIN-5AH的生长激素受体在非离子去污剂Triton X-100中被溶解。基于聚乙二醇沉淀生长激素:受体复合物的放射受体分析显示出时间依赖性和饱和性的激素结合。在去污剂溶液中,发现对约6 ng/ml的生物合成人生长激素的亲和力与完整的RIN细胞相似。所描述的溶解和受体分析条件对于进一步表征和纯化RIN细胞生长激素受体很有用,这可能为生长激素对胰岛β细胞作用的分子机制提供初步见解。