O'Brien T J, Gibbons W E, Nalick R H, Schlaerth J B, Morrow C P
J Clin Endocrinol Metab. 1981 Oct;53(4):698-702. doi: 10.1210/jcem-53-4-698.
Extracts of hydatidiform mole vesicles and the fluid contained in these vesicles were shown to contain a trophoblastic androgen binding protein. This protein was found to be distinct from serum testosterone-estradiol binding globulin (TEBG) by its isoelectric point, its affinity for dihydrotestosterone (DHT) and by Concanavalin A binding. The elution pH of this binding protein was shown to be 4.6, whereas that of TEBG was pH 5.2-5.3. The apparent dissociation constant (Kd app) for TEBG as determined by Scatchard analysis was 2.0 X 10(-9) M, whereas the Kd app for the trophoblastic binding protein after isoelectric focusing was 1.5 X 10(-10) M. A second binding protein found in both vesicular extracts and mole fluid was shown to have an isoelectric elution value (pH 5.2) similar to TEBG and an Kd app of 1.7 X 10(-9) M DHT, very close to the TEBG value. Apparent equilibration for both proteins with DHT was shown to occur in approximately 4H, and both proteins were shown to be high affinity, low capacity binders. The relative affinities of both proteins for other steroids was found to be similar except for methyltrienolone, which appeared to have a higher affinity for the trophoblastic binding protein.
葡萄胎水泡及其水泡内所含的液体提取物被证明含有一种滋养层雄激素结合蛋白。通过其等电点、对双氢睾酮（DHT）的亲和力以及伴刀豆球蛋白A结合情况，发现这种蛋白与血清睾酮 - 雌二醇结合球蛋白（TEBG）不同。这种结合蛋白的洗脱pH值显示为4.6，而TEBG的洗脱pH值为5.2 - 5.3。通过Scatchard分析测定，TEBG的表观解离常数（Kd app）为2.0×10⁻⁹ M，而异电聚焦后滋养层结合蛋白的Kd app为1.5×10⁻¹⁰ M。在水泡提取物和葡萄胎液中发现的第二种结合蛋白，其等电洗脱值（pH 5.2）与TEBG相似，DHT的Kd app为1.7×10⁻⁹ M，非常接近TEBG的值。两种蛋白与DHT的表观平衡在大约4小时内出现，并且两种蛋白都显示为高亲和力、低容量结合剂。除了甲基三烯醇酮外，发现两种蛋白对其他类固醇的相对亲和力相似，甲基三烯醇酮似乎对滋养层结合蛋白具有更高的亲和力。
