Abstract
Specific activity and kinetic constants of trypsin from the pyloric caeca of two strains of rainbow trout, Salmo gairdneri, were measured using α-N-benzoyl-DL-arginine-ρ-nitroaniline∙HCl No increase in activity was observed with cold acclimation, suggesting that cold acclimation induces no increase in trypsin concentration. The apparent Km for the substrate was independent of assay temperature over the physiological range in both strains, probably to maintain high rates of catalysis at higher temperatures when nutrient requirements are high. Strain A trout produced a trypsin with lower affinity on cold acclimation, but Strain B trout did not. The two strains differed in intestinal morphology as well as in the characteristics of their trypsins.
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