Tryptic digestion of catalase (H 2O 2:H 2O 2 oxidoreductase, EC 1.11.1.6) leads to a gradually increased peroxidatic activity towards phenolic compounds. The reactivity with ethylhydroperoxide increases 2–3 times after brief digestion but decreases thereafter. The catalatic activity and the reactivity with methylhydroperoxide disappear rapidly. The results indicate a loosening of the structure around the hematins, increasing the reactivity with peroxide and hydrogen donor substrates formerly sterically hindered. This change may occur to some extent without loss of the catalase-specific ability to react rapidly with hydroperoxides. The ability to peroxidize ethanol is apparently not loss before the loss of high reactivity with hydroperoxides. After brief exposure of catalase to pH > 12 leading to its dissociation into subunits, the enzyme recombines when the pH is lowered (Samejima, T., McCabe, W. J. and Tsi Yang, J. (1968) Arch. Biochem. Biophys. 127, 354–360). After this procedure most (∼ 70%) of the catalatic activity is recovered. The reactivity with ethylhydroperoxide is doubled and the peroxiding actifvity towards phenolic compounds is strongly increased. The results indicate an increased accessibility of the hematins of recombined catalase. However, they do not become reducible by dithionite. After longer exposure to high pH, all enzymic activities are decreased and the hematins become reducible.