scholarly journals Allometric scaling of hepatic biotransformation in rainbow trout

Author(s):  
Patrick N. Fitzsimmons ◽  
Alex D. Hoffman ◽  
Kellie A. Fay ◽  
John W. Nichols
1976 ◽  
Vol 33 (4) ◽  
pp. 666-675 ◽  
Author(s):  
Mark G. Pedersen ◽  
William K. Hershberger ◽  
Prince K. Zachariah ◽  
Mont R. Juchau

Six strains of rainbow trout (Salmo gairdneri), each geographically and genetically distinct, were compared in relation to their capacity for hepatic hydroxylation of aniline and benzo[a]pyrene, and reduction of p-nitrobenzoic acid to p-aminobenzoic acid, in vitro. The effects of 3-methylcholanthrene on stimulation of nitro reductase and aryl hydrocarbon hydroxylase were examined. For the three systems studied, a significant pattern was observed with respect to each strain’s capacity for metabolism. Induction experiments suggested that environment may influence gene expression. Enzyme kinetics and spectral properties were also examined, and mechanisms causing variability within and among strains were discussed.


1980 ◽  
Vol 37 (9) ◽  
pp. 1450-1453 ◽  
Author(s):  
J. F. Klaverkamp ◽  
B. R. Hobden

Two factors, potency of brain acetylcholinesterase (AChE) inhibition and biotransformation by liver homogenate, were investigated to understand the temperature-dependent toxicity of fenitrothion (FTN) in rainbow trout (Salmo gairdneri) and the 600- to 1000-fold differences in concentration between FTN and another organophosphate (OP) insecticide, acephate (ATE), required to produce death in these trout. Concentrations required to produce 50% inhibition of brain AChE were similar for ATE and FTN, ~125 mmol/L and 80 mmol/L, respectively, whereas fenitrooxon (FTO), the oxidative desulfuration metabolite of FTN, was approximately five orders of magnitude more potent. Incubation with liver homogenate, however, demonstrated that a more potent brain AChE inhibitor was produced from ATE, but not from FTN. It is concluded that hepatic biotransformation of FTN to FTO does not explain previous observations of FTN temperature dependency and differences in concentrations producing lethality.Key words: acephate, acetylcholinesterase, biotransformation, brain, fenitrothion, fenitrooxon, liver


Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
A Ghasemi Pirbalouti ◽  
E Pirali ◽  
G Pishkar ◽  
S Mohammadali Jalali ◽  
M Reyesi ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document