Shani J, Barkey R J, Amit T
J Recept Res. 1981;2(4):407-17. doi: 10.3109/107998981809038875.
The specific binding of lactoperoxidase-labelled 125I-labelled ovine prolactin was determined in a membrane particulate of the pigeon crop-sac mucosal epithelium. Binding was found to be dependent upon the particulate preparation used, its protein concentration and the length of the incubation at 5 degrees C. Scatchard analysis of the binding to crop-sacs from saline or prolactin-injected (1.9 microgram per pigeon) revealed that prolactin stimulated 7-fold its own receptors by increasing the number of binding sites per mg protein: saline - 392 +/- 75 fmol/mg protein and prolactin 2736 +/- 602 fmol/mg protein (p less than 0.01). This increase did not affect the affinity constant (Ka): saline - 5.28 +/- 0.75 x 10(8) l/mol and prolactin 3.28 +/- 0.40 x 10(8) l/mol (N.S.), in keeping with the stimulatory effect of prolactin in the rat liver and mammary glands. This study further demonstrates the physiological role of endogenous prolactin in maintaining its own binding-sites in the pigeon crop-sac, since the administration of 0.8 ml anti-serum to prolactin resulted in a 63% reduction in the specific binding of labelled hormone in vitro. These results confirm the prolactin binding to the pigeon crop-sac mucosa, quantify the stimulation of this binding by prolactin itself, and demonstrate the role of the endogenous hormone in the maintenance of these receptors.
在鸽嗉囊黏膜上皮的膜微粒中测定了乳过氧化物酶标记的¹²⁵I标记的绵羊催乳素的特异性结合。发现结合取决于所用的微粒制剂、其蛋白质浓度以及在5℃下的孵育时间。对来自生理盐水处理或注射催乳素(每只鸽1.9微克)的嗉囊的结合进行Scatchard分析表明,催乳素通过增加每毫克蛋白质的结合位点数量,使其自身受体增加了7倍:生理盐水组 - 392±75飞摩尔/毫克蛋白质,催乳素组 - 2736±602飞摩尔/毫克蛋白质(p<0.01)。这种增加不影响亲和常数(Ka):生理盐水组 - 5.28±0.75×10⁸升/摩尔,催乳素组 - 3.28±0.40×10⁸升/摩尔(无显著差异),这与催乳素在大鼠肝脏和乳腺中的刺激作用一致。本研究进一步证明了内源性催乳素在维持其在鸽嗉囊中自身结合位点方面的生理作用,因为给予0.8毫升催乳素抗血清导致体外标记激素的特异性结合减少了63%。这些结果证实了催乳素与鸽嗉囊黏膜的结合,量化了催乳素本身对这种结合的刺激,并证明了内源性激素在维持这些受体中的作用。