Preliminary data on PAH metabolism in the marine mussel Mytilus galloprovincialis from Arcachon Bay,France

Oxidation of polycyclic aromatic hydrocarbons (PAH) and epoxide-conjugation capacities were examined from mussels, Mytilus galloprovincialis, collected from a clean site at the entrance to Arcachon Bay (south-west France) in 1984, using subcellular preparations from whole bodies and digestive glands. The existence of low-cytochrome P-450-dependent oxygenase activities [cytochrome P-450 content, NADPH cytochrome c reductase and benzopyrene monooxygenase (BaPMO) activities] was confirmed, as well as the presence of a comparatively important capacity for epoxide conjugation [epoxide hydrolase (EH), glutathione S epoxide-transferase (GST) activities and total cytosolic-glutathione content]. The optimal incubation temperatures for the individual in vitro enzyme activities in the mussel (25°C for BaPMO, 31°C for EH and GST) were lower than that required for optimal mammalian enzyme activities. Except for cytochrome P-450 content, there was no significant difference in enzyme activities recorded in whole-body and digestive gland fractions.