Isolation and partial characterization of secreted hamster pituitary prolactin.
Isolation and partial characterization of secreted hamster pituitary prolactin.
复制标题
分泌的仓鼠垂体催乳素的分离和部分表征。
DOI：
10.1210/endo-108-3-850
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发表时间：
1981
期刊：
影响因子：
4.8
通讯作者：
F. Talamantes
中科院分区：
文献类型：
--
作者：
P. Colosi;E. Markoff;A. Levy;L. Ogren;N. Shine;F. Talamantes
由仓鼠前垂体分泌的PRL通过在Deae-Cellulose上的Sephadex G-100和离子交换色谱法上的凝胶过滤纯化。仓鼠PRL从Sephadex G-100洗脱，在DEAE-纤维素上，洗脱体积与空隙体积比为1.85，盐浓度为0.13 m NaCl。在几种凝胶系统中证明了激素的电泳均匀性，并且在硫酸钠存在下电泳表明分子量为22,000 +/- 2,000。仓鼠PRL与抗血清与小鼠PRL没有反应。仓鼠PRL在体外小鼠乳腺测定法中表现出乳脂活性。仓鼠PRL从哺乳动物乳腺受体中移位[125i] iodo-prl。因此，关于其在Sephadex G-100上的排除特性，其分子量及其生物学活性，仓鼠PRL与其他哺乳动物PRL非常相似。
PRL secreted by hamster anterior pituitaries was purified by gel filtration on Sephadex G-100 and ion exchange chromatography on DEAE-cellulose. Hamster PRL eluted from Sephadex G-100 with an elution volume to void volume ratio of 1.85 and at a salt concentration of 0.13 M NaCl on DEAE-cellulose. Electrophoretic homogeneity of the hormone was demonstrated in several gel systems, and electrophoresis in the presence of sodium dodecyl sulfate indicated a molecular weight of 22,000 +/- 2,000. Hamster PRL did not cross-react with antiserum to mouse PRL. Hamster PRL displayed lactogenic activity in an in vitro mouse mammary gland assay. Hamster PRL displaced [125I]iodo-PRL from lactating rabbit mammary gland receptors. Thus, with respect to its exclusion properties on SEphadex G-100, its molecular weight, and its biological activity, hamster PRL closely resembles other mammalian PRLs.