Isolation and purification of glutathione S-transferases from Brachionus plicatilis and B. calyciflorus (Rotifera).
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. 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.
Bowman
B P
BP
Division of Science, University of Tampa, FL 33606.
Snell
T W
TW
Cochrane
B J
BJ
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000302:isolation & purification* / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism; D008970:Molecular Weight; D012403:Rotifera / Q000201:enzymology*
D007527:Isoenzymes; D005982:Glutathione Transferase