Hanks M C, Talbot R T, Sang H M
AFRC Institute of Animal Physiology and Genetics Research, Roslin, Midlothian.
J Mol Endocrinol. 1989 Jul;3(1):15-21. doi: 10.1677/jme.0.0030015.
The putative chicken prolactin (chPRL) cDNA clone PRL101 was manipulated in vitro and cloned into the Escherichia coli expression vector pKK2332 to produce a plasmid coding for recombinant-derived mature chPRL (R-chPRL). Expression of this manipulated cDNA sequence in E. coli resulted in the production of a 23 kDa protein which cross-reacted with specific chPRL antisera in Western blots. The partially purified protein stimulated ring dove crop sac mucosa to proliferate in a PRL bioassay, demonstrating that the R-chPRL was biologically active. R-chPRL was expressed at a level of approximately 1.5% of total cell protein.
对假定的鸡催乳素（chPRL）cDNA克隆PRL101进行体外操作，并将其克隆到大肠杆菌表达载体pKK2332中，以产生编码重组衍生成熟chPRL（R-chPRL）的质粒。该操作后的cDNA序列在大肠杆菌中的表达产生了一种23 kDa的蛋白质，该蛋白质在蛋白质免疫印迹中与特异性chPRL抗血清发生交叉反应。在PRL生物测定中，部分纯化的蛋白质刺激了环鸽嗉囊黏膜增殖，表明R-chPRL具有生物活性。R-chPRL的表达水平约占总细胞蛋白的1.5%。
