Paloma de la Llosa-Hermier M, Hermier C, de la Llosa P
Acta Endocrinol (Copenh). 1976 Oct;83(2):393-401. doi: 10.1530/acta.0.0830393.
The binding of luteinizing hormone (LH) to cow corpora lutea homogenates was studied using a tritium labelled hormone obtained by reductive methylation. The KD observed was 0.9 10(-10) M and the number of sites was the equivalent of 0.4 10(-15) moles per mg of wet tissue. The influence of the pH and temperature was examined. HCG and LH produced the same binding inhibition properties of the derivative used for labelling LH were similar to those of native LH. The inhibitory activity of the subunits was extremely low (alpha-LH: 4%, beta-LH: 1%). No significant inhibition was observed in the case of FSH or prolactin.
利用通过还原甲基化获得的氚标记激素,研究了促黄体生成素(LH)与牛黄体匀浆的结合。观察到的解离常数(KD)为0.9×10⁻¹⁰ M,结合位点数量相当于每毫克湿组织0.4×10⁻¹⁵ 摩尔。研究了pH值和温度的影响。人绒毛膜促性腺激素(HCG)和LH产生相同的结合抑制特性,用于标记LH的衍生物与天然LH相似。亚基的抑制活性极低(α-LH:4%,β-LH:1%)。在促卵泡生成素(FSH)或催乳素的情况下未观察到明显抑制作用。