Lai Z N, Emtner M, Roos P, Nyberg F
Department of Pharmaceutical Pharmacology, University of Uppsala, Sweden.
Brain Res. 1991 Apr 19;546(2):222-6. doi: 10.1016/0006-8993(91)91485-j.
The ability to bind iodine-labelled human growth hormone ([125I]hGH) was measured in different parts of the human brain. The choroid plexus contained the highest amount of binding sites (receptors) and was therefore selected for further studies. The binding between [125I]hGH and the receptor was saturable, of high affinity (Ka = 0.63 nM-1) and pH- as well as time-dependent. After solubilization with Triton X-100 the receptors retained their hormone-binding properties and eluted in the high molecular weight range (greater than 500,000) upon molecular sieve chromatography. Analysis by an affinity cross-linking technique indicated a hormone-binding unit of molecular weight 51,000. The molecular characteristics of the identified binding sites are discussed in comparison to those of growth hormone receptors of human and animal origin.
在人脑的不同部位测量了结合碘标记的人生长激素（[125I]hGH）的能力。脉络丛含有最高量的结合位点（受体），因此被选作进一步研究对象。[125I]hGH与受体之间的结合是可饱和的，具有高亲和力（Ka = 0.63 nM-1），且依赖于pH值和时间。用Triton X-100溶解后，受体保留了其激素结合特性，并在分子筛色谱中以高分子量范围（大于500,000）洗脱。亲和交联技术分析表明激素结合单元的分子量为51,000。将所鉴定结合位点的分子特征与人及动物来源的生长激素受体的特征进行了比较讨论。
