Glycosylated human prolactin.
Glycosylated human prolactin.
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DOI：
10.1210/endo-116-1-359
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发表时间：
1985
期刊：
影响因子：
4.8
通讯作者：
U. Lewis;R. Singh;Y. Sinha;W. Vanderlaan
中科院分区：
文献类型：
--
作者：
U. Lewis;R. Singh;Y. Sinha;W. Vanderlaan
从垂体中分离出一种糖基化的人催乳素（G-hPRL）。在小扁豆凝集素-Sepharose 4 B柱上从主要形式的PRL中分离出糖蛋白。PRL的主要形式没有结合到小扁豆凝集素，而糖基化修饰，并可以洗脱甲基-α-D-甘露吡喃糖苷。通过在十二烷基硫酸钠中的凝胶电泳，估计糖基化PRL的mol wt为25，000。hPRL的mol wt为23，000。在hPRL的RIA中，糖基化激素的反应性约为主要形式的三分之一。由于hPRL中只有一个Asn-X-Ser（Thr）序列，因此31位的天冬酰胺可能是N-连接糖基化的位点。
A glycosylated form of human PRL (G-hPRL) was isolated from pituitary glands. The glycoprotein was separated from the major form of PRL on columns of lentil lectin-Sepharose 4B. The major form of PRL did not bind to the lentil lectin, whereas the glycosylated modification did and could be eluted with methyl-alpha-D-mannopyranoside. By gel electrophoresis in sodium dodecyl sulfate, a mol wt of 25,000 was estimated for the glycosylated PRL. The mol wt of hPRL is 23,000. In a RIA for hPRL, the glycosylated hormone was about one third as reactive as the principal form. Since there is only one Asn-X-Ser(Thr) sequence in hPRL, the asparagine at position 31 is the likely point of N-linked glycosylation.