Oestrogen sulfotransferase: isolation of a high specific activity species from bovine placenta.

S S Moore, E O Thompson, A R Nash
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引用次数: 12

Abstract

During the course of a study of the control of expression of steroid-binding proteins in human mammary cancer oestrogen sulfotransferase was isolated from bovine placenta. By a combination of salt precipitation and ion-exchange and gel-permeation chromatography two forms of the enzyme were isolated. The forms, which apparently differ only in charge, have specific activities 100-300 times greater than has previously been reported for the enzyme. Partial peptide sequences of these enzymes are presented.

从牛胎盘中分离出一种高比活性的雌激素硫转移酶。
在研究控制人乳腺癌中类固醇结合蛋白的表达过程中,从牛胎盘中分离出雌激素硫转移酶。通过盐沉淀、离子交换和凝胶渗透色谱相结合的方法分离出两种形式的酶。这两种形式显然只是在电荷上有所不同,它们的特定活性比以前报道的酶高100-300倍。给出了这些酶的部分肽序列。
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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