Purification and partial characterization of prolactin from the California ground squirrel (Spermophilus beecheyi).
Purification and partial characterization of prolactin from the California ground squirrel (Spermophilus beecheyi).
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加州地松鼠 (Spermophilus beecheyi) 催乳素的纯化和部分表征。
DOI：
10.1095/biolreprod36.4.1017
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发表时间：
1987
影响因子：
3.6
通讯作者：
Talamantes,F
中科院分区：
文献类型：
--
作者：
Colosi,P;Holekamp,KE;Thordarson,G;Southard,JN;Talamantes,F
用Sephadex G-100凝胶过滤和Polybuffer exchange94离子交换色谱法纯化了培养的地鼠垂体分泌的催乳素（Prl）。从190个垂体的培养基中纯化得到纯化的SbPrl 1.1 mg。经聚丙烯酰胺凝胶电泳，在十二烷基硫酸钠存在下，SbPrl的表观分子量为27000，等电点为6.3，不含任何天冬酰胺连接的碳水化合物。纯化的SbPrl取代了泌乳兔乳腺膜上结合位点的251标记的羊Prl，并刺激培养的小鼠乳腺上皮细胞分泌a-乳蛋白。
Prolactin (Prl) secreted by cultured ground squirrel (Spermophilus beecheyi) pituitaries (SbPrl) was purified by gel filtration on Sephadex G-100 and ion-exchange chromatography on Polybuffer Exchanger 94. Purification from culture medium from 190 pituitaries yielded 1.1 mg of purified SbPrl. The SbPrl has an apparent molecular weight of 27,000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, an isoelectric point of 6.3, and does not contain any asparagine-linked carbohydrate. Purified SbPrl displaces' 251-labeled ovine Prl from binding sites on lactating rabbit mammary gland membranes and stimulates secretion of a-lactalbumin by cultured mouse mammary gland epithelial cells.