Ward D N, Desjardins C, Moore W T, Nahm H S
Int J Pept Protein Res. 1979 Jan;13(1):62-70. doi: 10.1111/j.1399-3011.1979.tb01850.x.
The purification of rabbit lutropin is described. A product with a potency of 1.53 X NIH-LH-Sl was obtained as assayed by the ovarian ascorbic acid depletion assay. In a homologous radioimmunoassay, which is described, rabbit lutropin has a potency 4.83 X NIH-LH-Sl. In a radioligand assay, utilizing labeled ovine lutropin as the trace, the relative potency was 0.47 X NIH-LH-Sl measured by 50% inhibition comparison since rabbit lutropin response in this system did not parallel ovine lutropin. A counter-current distribution procedure for separation of rabbit lutropin subunits is described. Amino acid composition of the isolated subunits and intact rabbit lutropin was determined. The carbohydrate composition of the latter is presented; only amino sugar determinations are available for the subunits. The NH2-terminal amino acids are phenylalanine (alpha subunit) and alanine (beta subunit). Preliminary data on COOH-terminal amino acids are provided.
本文描述了兔促黄体素的纯化过程。通过卵巢抗坏血酸耗竭试验测定，获得了效价为1.53×NIH-LH-S1的产品。在所描述的同源放射免疫测定中，兔促黄体素的效价为4.83×NIH-LH-S1。在以标记的羊促黄体素为示踪剂的放射配体测定中，由于该系统中兔促黄体素的反应与羊促黄体素不平行，通过50%抑制比较测得相对效价为0.47×NIH-LH-S1。本文还描述了一种用于分离兔促黄体素亚基的逆流分配方法。测定了分离出的亚基和完整兔促黄体素的氨基酸组成。给出了后者的碳水化合物组成；亚基仅提供了氨基糖的测定结果。NH2末端氨基酸分别为苯丙氨酸（α亚基）和丙氨酸（β亚基）。提供了关于COOH末端氨基酸的初步数据。
