Xenobiotic biotransformation in aquatic organisms Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/gh93h171m

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  • Aquatic animals are exposed to a variety of natural and anthropogenic xenobiotics. Biotransformation of xenobiotics was examined in three aquatic animals: a primitive mollusc (chiton); a shellfish which is an important human food source (oyster); and, a lower vertebrate model for toxicological studies (rainbow trout). Since digestive glands of Cryntochiton stelleri possessed cytochrome P-450 (P-450), various Phase II conjugation and flavin-containing monooxygenase (FMO) activities, primitive marine molluscs have the appropriate enzymes to cope with organic xenobiotics. Studies examining gill and visceral mass microsomes from the oyster (Crassostrea gigas) demonstrated strong evidence for FMO and co-oxidation pathways and possible involvement of P- 450. FMO and one electron co-oxidation pathways appear to catalyze N-oxidation of 2-aminofluorene in microsomes from oyster visceral mass suggesting that, like the chiton, multiple enzymes are involved in xenobiotic biotransformation in the oyster. In rainbow trout, (Oncorhynchus mykiss), the in vitro and in vivo biotransformation of aldicarb was examined to help determine the role of FMO in this species. Since FMO was responsible for the formation of the major metabolite, aldicarb sulfoxide, this enzyme plays a significant role in the biotransformation of nitrogen and sulfur-containing chemicals. FMO enzyme activity was used in conjunction with immunochemical quantitation to observe the tissue distribution, sexual and developmental differences of trout FMO. Immunoquantitation of FMO was directly correlated with enzyme activity. These data showed that trout FMO is structurally and biochemically related the mammalian forms of FMO. Since the trout has been used as an alternative vertebrate model to study mammalian toxicology, the demonstration of FMO in this species will provide a better understanding of the enzymatic basis for the biotransformation of nitrogen and sulfur-containing chemicals.
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