Metabolism of endogenous and xenobiotic aldehydes by rainbow trout (Oncorhynchus mykiss) liver fractions
Aldehyde dehydrogenase (ALDH) specific activity was measured in crude homogenates, post-mitochondrial supernatants, cytosolic and microsomal fractions of trout liver, using a number of endogenous and xenobiotic aldehydes and both NAD+ and NADP+ as co-factors. All the activity found in the crude homogenate could be accounted for by the sum of the cytosolic and microsomal activities. Highest activities were found with the medium chain length substrates hexanal and nonanal in all fractions. The α,β-unsaturated aldehydes, (E,E)-2,4-nonadienal-1-al, and trans, trans-2,4-decadienal, were also good substrates for both fractions, while the hydroxylated α,β unsaturated trans-4-hydroxy-2-nonenal was a good substrate only for the microsomal fraction. Short chain and aromatic xenobiotic substrates were metabolized at much lower rates, and only the microsomal fraction was effective against acetaldehyde, acrolein, and benzaldehyde. Neither fraction metabolized 2,5-dihydroxy benzaldehyde. NAD+ was the preferred co-factor for most substrates. Apparent affinity (K
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- Toxicology
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- 34 Chemical sciences
- 31 Biological sciences
- 06 Biological Sciences
- 05 Environmental Sciences
- 03 Chemical Sciences
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Related Subject Headings
- Toxicology
- 41 Environmental sciences
- 34 Chemical sciences
- 31 Biological sciences
- 06 Biological Sciences
- 05 Environmental Sciences
- 03 Chemical Sciences