Abstract
A modification of the Sumner and Dounce method of preparing crystalline ox-liver catalase was developed which yielded a product with a specific activity (Kat. f) of 72,000. It was demonstrated by a solubility test technic that the product contained 2 distinct catalases with Kat''f. values of 45,000 and 180,000. It was suggested that the catalase with the Kat. f. value of 180,000 is attached to insoluble complexes in the liver cell and is the structural catalase of liver. A protein exhibiting a reversible change in solubility on exposure to radiation of wave lengths in the visible and u.-v. regions of the spectrum was detected in partially purified catalase prepns.