ISOLATION AND PURIFICATION OF GLUTATHIONE S-TRANSFERASES FROM BRACHIONUS-PLICATILIS AND BRACHIONUS-CALYCIFLORUS (ROTIFERA)

被引:6
作者
BOWMAN, BP
SNELL, TW
COCHRANE, BJ
机构
[1] UNIV TAMPA, DIV SCI, TAMPA, FL 33606 USA
[2] UNIV S FLORIDA, DEPT BIOL, TAMPA, FL 33620 USA
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1990年 / 95卷 / 03期
关键词
D O I
10.1016/0305-0491(90)90031-N
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
1. 1. 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. 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. 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. 4. Rotifer GSTs are unusual because they are monomers whereas all other animals thus far investigated possess dimeric GSTs. © 1990.
引用
收藏
页码:619 / 624
页数:6
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