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猪肝中L-丝氨酸O-硫酸盐降解系统的纯化及性质

The purification and properties of the L-serine O-sulphate degrading system of pig liver.

作者信息

Tudball N, Thomas P, Bailey-Wood R

出版信息

Biochem J. 1971 Mar;121(5):747-52. doi: 10.1042/bj1210747.

Abstract
  1. The enzyme system from pig liver responsible for the alphabeta-elimination of l-serine O-sulphate was purified 1000-fold. 2. Isoelectric focusing produced two enzymically active fractions with isoelectric points at pH5.6 and 5.9 respectively. 3. Osmometry and gel filtration showed both enzymes to possess molecular weights of approx. 54000. 4. The separate activities exhibited similar amino acid compositions.
摘要
  1. 负责从L-丝氨酸O-硫酸盐中进行αβ消除反应的猪肝酶系统被纯化了1000倍。2. 等电聚焦产生了两个具有酶活性的组分,其等电点分别为pH5.6和5.9。3. 渗透压测定和凝胶过滤表明这两种酶的分子量均约为54000。4. 各自的活性表现出相似的氨基酸组成。

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本文引用的文献

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Endogenous sulphate acceptors in rat liver.大鼠肝脏中的内源性硫酸盐受体
Biochem J. 1960 Nov;77(2):294-304. doi: 10.1042/bj0770294.

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