Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
