Aragona C, Friesen H G
Endocrinology. 1975 Sep;97(3):677-84. doi: 10.1210/endo-97-3-677.
Specific binding sites for prolactin have been detected in membrane preparations from the testis, epididymis, seminal vesicles and prostate of male rats. The binding was time and temperature dependent. In prostatic tissue the binding of prolactin was a saturable process with an association constant (Ka) of 3 X 10(9) M-1 and a binding capacity of 125 femtomoles per mg of protein. The binding of prolactin to the prostate was inhibited only by lactogenic hormones. In the testis the low binding of prolactin increased slightly from 20 to 70 days of age. On the other hand, in the prostate the highest specific binding was found in membrane preparation from 20-day-old rats while 270-day-old rats had only 10% as much specific binding. The administration of estrogen also lowered prolactin binding to prostatic membranes. Castration caused an even greater decrease in the binding of [125I] iodo PRL in the prostate whereas in the liver this procedure resulted in a major increase in the binding of labeled prolactin.
在雄性大鼠的睾丸、附睾、精囊和前列腺的膜制剂中已检测到催乳素的特异性结合位点。这种结合具有时间和温度依赖性。在前列腺组织中，催乳素的结合是一个可饱和的过程，其缔合常数（Ka）为3×10⁹ M⁻¹，每毫克蛋白质的结合容量为125飞摩尔。催乳素与前列腺的结合仅受促乳激素抑制。在睾丸中，催乳素的低结合率在20至70日龄时略有增加。另一方面，在前列腺中，20日龄大鼠的膜制剂中特异性结合最高，而270日龄大鼠的特异性结合仅为其10%。雌激素的给药也降低了催乳素与前列腺膜的结合。去势导致前列腺中[¹²⁵I]碘催乳素的结合进一步大幅下降，而在肝脏中，该操作导致标记催乳素的结合大幅增加。
