Cytosolic epoxide hydrolase in fetal and adult human liver

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Abstract
The epoxide hydrolase and glutathione S-transferase activity towards styrene oxide as substrate were investigated and compared in fetal and adult human liver cytosols. The rate of formation of styrene glycol from styrene oxide (nmole/min/mg protein) was 0.23±0.02 (¯x±SE;n=10) in fetal and 0.83±0.05 (¯x±SE;n=14) in adult liver specimens. The enzyme followed Michealis-Menten kinetics in the fetal liver. In adult liver specimens the enzyme showed biphasic kinetics. For comparative purposes, the cytosolic glutathione S-transferase activity was investigated in the cytosolic fractions from the same liver specimens. The fetal activity was 40% of the adult activity 3.9±0.50 (¯x±SE;n=10) versus 9.94±1.75 (¯x±SE;n=14) nmoles/min/mg protein.