Giudice L C, Pierce J G
Endocrinology. 1977 Sep;101(3):776-81. doi: 10.1210/endo-101-3-776.
Electrophoretic patterns of intact human and bovine TSH and bovine LH can be clearly distinguished from those of their subunits in 12% polyacrylamide gels, thus providing an easy method of examining subunit recombination. Two distinct components of both bovine and human TSH-beta subunits are observed, of which only one recombines with alpha subunits. Both beta-components cross-react with antisera to TSH and TSH-beta and have, within experimental error, identical amino acid compositions. Thus, the non-recombining component is a non-functional form of TSH-beta which has retained its immunological specificity, and the data explain why the recovery of biological activity during the recombination of TSH subunits is substantially less than with several other glycoprotein hormone preparations.
在12%的聚丙烯酰胺凝胶中，完整的人促甲状腺激素（TSH）、牛促甲状腺激素和牛促黄体生成素（LH）的电泳图谱可与它们的亚基的电泳图谱清晰区分，从而提供了一种检测亚基重组的简便方法。观察到牛和人促甲状腺激素β亚基都有两个不同的组分，其中只有一个能与α亚基重组。两种β组分都能与抗促甲状腺激素和促甲状腺激素β的抗血清发生交叉反应，并且在实验误差范围内，它们的氨基酸组成相同。因此，不发生重组的组分是促甲状腺激素β的一种无功能形式，它保留了其免疫特异性，这些数据解释了为什么促甲状腺激素亚基重组过程中生物活性的恢复明显低于其他几种糖蛋白激素制剂。
