促黄体生成素受体：人促黄体生成素与黄体化大鼠卵巢匀浆的特异性结合。
Luteinizing hormone receptors: specific binding of human luteinizing hormone to homogenates of luteinized rat ovaries.
作者信息
Lee C Y, Ryan R J
出版信息
Proc Natl Acad Sci U S A. 1972 Dec;69(12):3520-3. doi: 10.1073/pnas.69.12.3520.
Abstract
Binding of human [(125)I]luteinizing hormone to homogenates of luteinized rat ovaries is dependent upon time, temperature, and pH and is saturable. Injection of human chorionic gonadotropin in vivo or addition of unlabeled human chorionic gonadotropin or human or ovine luteinizing hormone in vitro inhibits binding, whereas follicle stimulating hormone or prolactin is without effect. The dissociation constant for binding of luteinizing hormone receptor is 0.79 nM. The number of binding sites is 94 femtomol/mg of wet weight. NaCl, KCl, MgSO(4), and CaCl(2) at concentrations below 10 mM have no effect on binding, while all salts significantly inhibit binding at 150 mM. Binding of [(125)I]luteinizing hormone to its receptors is destroyed by proteolytic enzymes and by phospholipase C and D. The total binding activity is quantitatively recovered in the 2000 x g pellet of the homogenate.
摘要
人[¹²⁵I]促黄体生成素与黄体化大鼠卵巢匀浆的结合取决于时间、温度和pH，且具有饱和性。体内注射人绒毛膜促性腺激素或体外添加未标记的人绒毛膜促性腺激素、人或羊促黄体生成素会抑制结合，而促卵泡激素或催乳素则无此作用。促黄体生成素受体结合的解离常数为0.79 nM。结合位点的数量为94飞摩尔/毫克湿重。浓度低于10 mM的NaCl、KCl、MgSO₄和CaCl₂对结合无影响，而所有盐在150 mM时均显著抑制结合。[¹²⁵I]促黄体生成素与其受体的结合会被蛋白水解酶、磷脂酶C和D破坏。总结合活性在匀浆的2000×g沉淀中可定量回收。
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