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. Author manuscript; available in PMC: 2011 Jun 15.
Published in final edited form as: Biochem J. 2010 May 27;428(3):419–427. doi: 10.1042/BJ20091863

Table 1.

Activities of recombinant GSTs from various species

Enzyme substrate PcpF PcpF C53S Re-YqjG Ec-YqjG ECM4 hGSTO1-1 hGSTO2-2
CDNB ND ND ND ND ND 0.02 ± 0.01 0.01 ± 0.01
Ethacrynic acid 0.09 ± 0.01 0.11 ± 0.01 0.26 ± 0.05 0.07 ± 0.01 0.13 ± 0.01 0.02 ± 0.01 0.37 ± 0.06
GS-TriCH 2.66 ± 0.12 ND 1.67 ± 0.13 1.76 ± 0.07 3.18 ± 0.06 ND ND
HED 23.1 ± 0.8 ND 37.9 ± 0.8 9.54 ± 0.23 22.9 ± 0.3 3.91 ± 0.09 9.73 ± 0.08
DMAV 2.49 ± 0.31 ND 2.28 ± 0.13 1.30 ± 0.24 1.42 ± 0.17 0.074 ± 0.008 0.46 ± 0.02
DHA 1.91 ± 0.14 ND 1.71 ± 0.16 0.27 ± 0.03 0.88 ± 0.02 0.57 ± 0.01 26.5 ± 0.53
DiCPGS 0.22 ± 0.01 ND ND ND ND 1.56 ± 0.01 ND

Specific activities are reported as substrate consumed (μmol · min−1 · mg−1) of protein at 23 ± 1 °C and are means ± S.D. Assays were performed with 5 mM GSH except for the ethacrynic acid assay which used 1 mM GSH. ND, no apparent activity was detected; DiCPGS, S-(2′4′-dichlorophenacyl)glutathione.