Sinha Y N, Gilligan T A
Proc Soc Exp Biol Med. 1985 Apr;178(4):505-14. doi: 10.3181/00379727-178-42035.
Peptide mapping of individual pituitary proteins within the gel after separation by electrophoresis in NaDodSO4-polyacrylamide gels has revealed a high-molecular-weight (mol wt) protein whose fingerprint is similar to that of prolactin (PRL). This protein is approximately 4000 greater in mol wt than the traditional pituitary PRL, but does not appear to be the latter's prohormone. Its concentration ranged from 3 to 15% of the major PRL protein in the pituitary glands of several species examined. The protein isolated from sheep pituitary glands partly cross-reacted with a polyclonal antibody raised against the main PRL, but the material from mouse pituitary glands was completely noncross-reactive. The substance eluted from denaturing gels failed to significantly stimulate mucosal growth in the crop sac of the pigeons, a commonly used test for PRL's bioactivity. Its biological activities remain to be characterized.
在十二烷基硫酸钠-聚丙烯酰胺凝胶中进行电泳分离后，对凝胶内单个垂体蛋白进行肽图分析，发现了一种高分子量（分子量）蛋白，其指纹图谱与催乳素（PRL）相似。这种蛋白的分子量比传统垂体PRL大约大4000，但似乎不是后者的前激素。在所检测的几种物种的垂体中，其浓度占主要PRL蛋白的3%至15%。从绵羊垂体中分离出的该蛋白与针对主要PRL产生的多克隆抗体有部分交叉反应，但从小鼠垂体中获得的物质则完全无交叉反应。从变性凝胶中洗脱的物质未能显著刺激鸽子嗉囊黏膜生长，而鸽子嗉囊黏膜生长是常用的PRL生物活性检测方法。其生物学活性仍有待确定。
