Studies on purification of oestrogen-induced protein from rat uterus and its physiological role in cultured cells.

Scientia Sinica Pub Date : 1979-02-01
L Yi-hsun
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Abstract

This paper presents evidence to show the presence of an oestrogen-induced protein (IP) from rat uterus which is able to stimulate the incorporation of 3H-thymidine into DNA of 3T6 fibroblasts in vitro. The purified uterine protein fraction has been shown th contain less than 10 detectable proteins. The molecular weight of IP band is about 50,000 Daltons with an iso-electric point of 4.5. Comparison of oestrogen-treated and -untreated uterine cytosols on SDS-acrylamide gel electrophoresis indicates that the IP band is also present in the untreated controls. It is therefore suggested that the oestrogen-induced protein may be analogous or identical to the growth-promoting protein synthesized by LX cells.

大鼠子宫雌激素诱导蛋白的纯化及其在体外培养细胞中的生理作用研究。
本文提出了一种来自大鼠子宫的雌激素诱导蛋白(IP)的证据,该蛋白能够刺激3h -胸苷结合到体外3T6成纤维细胞的DNA中。纯化后的子宫蛋白部分含有不到10种可检测的蛋白质。IP带的分子量约为50,000道尔顿,等电点为4.5。经sds -丙烯酰胺凝胶电泳比较,经雌激素处理和未处理的子宫细胞质也存在IP带。因此,雌激素诱导的蛋白可能与LX细胞合成的促生长蛋白类似或相同。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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