The rate with which n-butanol alters the properties of yeast catalase has been studied as a function of temperature and concentration of altering agent. Activation energies for catalase alteration lay within the rather narrow range of 20–23 kcal./mole, thus confirming a prediction made previously on the basis of the difference in energies of activation for heat destruction of altered and unaltered catalases. Alteration by optimal concentration of butanol was a reaction of zero order. Chloroform also altered yeast catalase with an activation energy within this range of μ values. The close agreement in μ values leads us to conclude that the action of these two altering agents, at all concentrations, is characterized by the same rate-limiting step, even though their action differs in other respects. It was concluded that catalase alteration is probably all-or-none on the molecular level, rather than on the cellular level. Alteration was invariably accompanied by a decrease in the size of the treated cells; alteration was sometimes accompanied by changes in the cytochrome spectrum, but there was no causal connection between these two events. These data are consistent with the interfacial hypothesis, which, in its present crude form, pictures alteration as consisting essentially in the desorption of catalase from some intracellular interface at which it is normally bound in the intact cell.
