从褶皱臂尾轮虫和萼花臂尾轮虫（轮虫纲）中分离和纯化谷胱甘肽S-转移酶

Isolation and purification of glutathione S-transferases from Brachionus plicatilis and B. calyciflorus (Rotifera).

Bowman B P, Snell T W, Cochrane B J

Division of Science, University of Tampa, FL 33606.

Comp Biochem Physiol B. 1990;95(3):619-24. doi: 10.1016/0305-0491(90)90031-n.

Abstract

The enzyme glutathione S-transferase (GST), a critical element in xenobiotic metabolism, was isolated from the marine rotifer Brachionus plicatilis and its freshwater congener B. calyciflorus. 2. In B. plicatilis, GST comprised 4.2% of cytosolic protein and was present as three separate isozymes with mol. wts 30,000, 31,400 and 33,700. Specific activity of crude homogenates was 56 nmol min-1 mg-1 protein, while that of affinity chromatography purified GST was 1850. 3. In B. calyciflorus, GST was present as two isozymes with mol. wts of 26,300 and 28,500, representing 1.0% of cytosolic protein. Crude GST specific activity was 1750 nmol min-1 mg-1 protein and purified was 72,400. 4. Rotifer GSTs are unusual because they are monomers whereas all other animals thus far investigated posses dimeric GSTs.

摘要

谷胱甘肽S-转移酶（GST）是外源生物代谢中的关键元素，已从海洋轮虫褶皱臂尾轮虫及其淡水同类萼花臂尾轮虫中分离出来。2. 在褶皱臂尾轮虫中，GST占胞质蛋白的4.2%，以三种分子量分别为30,000、31,400和33,700的独立同工酶形式存在。粗匀浆的比活性为56 nmol min-1 mg-1蛋白，而亲和层析纯化的GST的比活性为1850。3. 在萼花臂尾轮虫中，GST以两种分子量分别为26,300和28,500的同工酶形式存在，占胞质蛋白的1.0%。粗GST的比活性为1750 nmol min-1 mg-1蛋白，纯化后的比活性为72,400。4. 轮虫GST不同寻常，因为它们是单体，而迄今为止研究的所有其他动物都拥有二聚体GST。