Abstract
It is found empirically that a simple modification of the usual theoretical kinetic formulation (in which a transformation in the temperature scale is made) describes the temperature dependence of a wide variety of biochemical processes with a greater accuracy than hitherto achieved. Used in conjunction with the formulation of the theory of absolute reaction rates this empirical relation facilitates the determination of the thermodynamic functions. The results of applying these relations to biochemical processes support the contention that in the lower temperature range of enzyme activity a thermodynamic equilibrium exists between catalytically active and inactive forms of the enzyme.
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