{"refrec":{"BRefID":138116,"RR":"<b>Bowman, B.P.; Snell, T.W.; Cochrane, B.J.</b> (1990). Isolation and purification of glutathione s-transferases from <i>Brachionus plicatilis</i> and <i>B. Calyciflorus</i> (Rotifera). <i>Comp. Biochem. Physiol. (B Biochem. Mol. Biol.) 95(3)</i>: 619-624","BEntID":131846,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>Comp. Biochem. Physiol. (B Biochem. Mol. Biol.) 95(3)</i>: 619-624","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Bowman, B.P.; Snell, T.W.; Cochrane, B.J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Bowman, B.P.; Snell, T.W.; Cochrane, B.J.","Englishabstract":"1. The enzyme glutathione S-transferase (GST), a critical element in xenobiotic metabolism, was isolated from the marine rotifer <i>Brachionus plicatilis</i> and its freshwater congener <i>B. calyciflorus</i>. 2. In <i>B. plicatilis</i>, 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<sup>-1</sup> mg<sup>-1</sup> protein, while that of affinity chromatography purified GST was 1850. 3. In <i>B. calyciflorus</i>, 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<sup>-1</sup> mg<sup>-1</sup> 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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Isolation and purification of glutathione s-transferases from <i>Brachionus plicatilis</i> and <i>B. 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