The Journal of General Physiology · 1934 · 113 citations · 0 references
Life SciencesBiochemistryChemistryEnzymologyPhysical ChemistryCalorimetryChemical ThermodynamicsEnzyme KineticsProtein DenaturationDenaturationDenaturation KineticsDenaturation TemperatureEquilibriumHeat-induced DenaturationHeat-induced Protein DenaturationTemperature Effects On Enzyme Activity
There is a mobile equilibrium between the native and denatured forms of trypsin which depends on the concentrations of acid, alkali, and alcohol and on the temperature. The heat of denaturation in 0.01 N hydrochloric acid calculated from the effect of temperature on the equilibrium constant is -67,600 calories per mole.