THE EQUILIBRIUM BETWEEN ACTIVE NATIVE TRYPSIN AND INACTIVE DENATURED TRYPSIN

M. L. Anson, A. E. Mirsky

The Journal of General Physiology · 1934 · 113 citations · 0 references

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Abstract

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.