Record Details

Xenobiotic biotransformation in aquatic organisms

ScholarsArchive at Oregon State University

Field Value
Title Xenobiotic biotransformation in aquatic organisms
Names Schlenk, Daniel K. (creator)
Buhler, Donald R. (advisor)
Date Issued 1989-05-03 (iso8601)
Note Graduation date: 1989
Abstract 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.
Genre Thesis/Dissertation
Topic Cytochrome P-450
Identifier http://hdl.handle.net/1957/39367

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