Sakai S, Kohmoto K, Johke T
Endocrinol Jpn. 1975 Oct;22(5):379-87. doi: 10.1507/endocrj1954.22.379.
Prolactin iodinated by lactoperoxidase method showed immunologically, electrophoretically and biolo9gically similar properties to native prolactin and possessed enough specific radioactivity for receptor studies. 1251-prolactin was incubated with mouse mammary tissues at 8 days of lactation. Both binding and release of 1251-prolactin depended on incubation time and temperature and were maximal at 37 degrees C. Michaelis constant was estimated to be 1.4 X 10(-9) M from Lineweaver-Burk plot and to be 1.2 X 10(-9) M from id-value of the dose-response curve for displacement with native prolactin. Total number of binding sites for prolactin was 1.38 X 10(-15) mole per mg weight of tissue. Ovine prolactin, human growth hormone and human placental lactogen complete with 1251-prolactin and dose-response curves for these three hormones were all parallel. These results suggest the existence of a specific receptor site with high affinity for prolactin in lactating mouse mammary glands.
通过乳过氧化物酶法碘化的催乳素在免疫学、电泳学和生物学特性上与天然催乳素相似,并且具有足够的比放射性用于受体研究。将125I-催乳素与泌乳第8天的小鼠乳腺组织一起孵育。125I-催乳素的结合和释放均取决于孵育时间和温度,在37℃时达到最大值。根据Lineweaver-Burk图估计米氏常数为1.4×10(-9)M,根据用天然催乳素进行置换的剂量-反应曲线的id值估计为1.2×10(-9)M。催乳素结合位点的总数为每毫克组织重量1.38×10(-15)摩尔。绵羊催乳素、人生长激素和人胎盘催乳素与125I-催乳素竞争,这三种激素的剂量-反应曲线都是平行的。这些结果表明,泌乳小鼠乳腺中存在对催乳素具有高亲和力的特异性受体位点。