Pineal Gland Hydroxyindole-O-Methyl Transferase (HIOMT) From Rainbow Trout (Salmo gairdneri) Subject to Temperature-Dependent Substrate Inhibition by N-Acetylserotonin

1989 ◽  
Vol 7 (1) ◽  
pp. 31-36 ◽  
Author(s):  
Dougal J. Morton ◽  
Heather J. Forbes
Keyword(s):  
Rainbow Trout ◽  
Pineal Gland ◽  
Substrate Inhibition ◽  
Salmo Gairdneri ◽  
Temperature Dependent ◽  
Methyl Transferase

scholarly journals Coronary flow in a perfused rainbow trout heart

1987 ◽  
Vol 129 (1) ◽  
pp. 107-123 ◽  
Author(s):  
A. P. Farrell
Keyword(s):  
Rainbow Trout ◽  
Coronary Flow ◽  
Coronary Circulation ◽  
Coronary Vessels ◽  
Cardiac Metabolism ◽  
Salmo Gairdneri ◽  
Acclimation Temperature ◽  
Coronary Vascular Resistance ◽  
Coronary Resistance ◽  
Temperature Dependent

A preparation was developed to perfuse the coronary circulation in working hearts from rainbow trout (Salmo gairdneri Richardson). The preparation was used to examine pressure-flow relationships for the coronary circulation as the heart generated physiological and subphysiological work loads. Coronary vascular resistance increased exponentially as coronary flow rate decreased. Coronary resistance was also influenced by cardiac metabolism and acclimation temperature. When heart rate was increased, extravascular compression increased in coronary resistance. Direct vasoconstriction of the coronary vessels, produced by injections of adrenaline into the coronary circulation, was temperature-dependent.

Rheological properties of rainbow trout blood

1987 ◽  
Vol 65 (4) ◽  
pp. 879-883 ◽  
Author(s):  
Garth L. Fletcher ◽  
R. Tyson Haedrich
Keyword(s):  
Rainbow Trout ◽  
Shear Rate ◽  
Salvelinus Alpinus ◽  
Salmo Gairdneri ◽  
Pseudopleuronectes Americanus ◽  
Temperature Dependent ◽  
Shear Dependent Viscosity ◽  
Myoxocephalus Scorpius ◽  
Lower Temperature ◽  
Dependent Viscosity

The effects of shear rate and red cell concentration on the viscosity of rainbow trout (Salmo gairdneri) blood were evaluated at 0 and 15 °C using a cone-plate viscometer. The viscosity of blood was shear dependent at both temperatures, with the highest values occurring at the lower temperature and shear rate. The viscosity of plasma was not shear dependent. Viscosity of blood increased in a linear fashion between hematocrits of 0 and 40%. Viscosity of the rainbow trout blood was similar to that of arctic char (Salvelinus alpinus), but considerably lower and less shear and temperature dependent than the bloods of winter flounder (Pseudopleuronectes americanus) and shorthorn sculpin (Myoxocephalus scorpius). It is hypothesized that low shear and temperature dependent blood viscosity may be a characteristic of active fish.

Brain Acetylcholinesterase Inhibition and Hepatic Activation of Acephate and Fenitrothion in Rainbow Trout (Salmo gairdneri)

1980 ◽  
Vol 37 (9) ◽  
pp. 1450-1453 ◽  
Author(s):  
J. F. Klaverkamp ◽  
B. R. Hobden
Keyword(s):  
Rainbow Trout ◽  
Liver Homogenate ◽  
Acetylcholinesterase Inhibition ◽  
Salmo Gairdneri ◽  
Ache Inhibitor ◽  
Temperature Dependent ◽  
Brain Ache ◽  
Two Factors ◽  
Brain Acetylcholinesterase ◽  
Hepatic Biotransformation

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

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