Growth of originally aerobic bakers' yeast under conditions of anaerobiosis caused a decrease in the total specific catalatic activity (patent plus cryptic) of one-half per generation. It is concluded that reversion of catalase was a dilution, rather than a destruction, of the intracellular enzyme. However, the specific patent (whole cell) catalase activity remained constant for one or more generations, and then declined at a considerably slower rate than did the total activity. Thus the cryptic factor diminished progressively during anaerobic growth; after seven or eight generations virtually all the catalase was patent;i.e., the cryptic factor (the ratio of total enzyme to patent enzyme) was approximately unity. At this point, the basal level of enzyme was attained, and thereafter maintained by a basal synthesis, which produced only the patent, heatstable, variety. Aerobic growth caused a significant, but much smaller, decline of both total catalase activity and of the cryptic factor. The data suggested that during reversion, the cryptic, heat-labile catalase became progressively converted to the patent, heat-resistant form. A model of these events is presented.
I N T R O D U C T I O NAn inducible enzyme is one whose rate of synthesis is increased greatly by the presence of a specific inducer. Chantrenne and Courtois (1) demonstrated that yeast catalase was an inducible enzyme, and that its inducer was oxygen, or possibly hydrogen peroxide formed by reduction of oxygen by cell metabolism.When a population of previously "induced" cells is allowed to grow in absence of the inducer, the rate of synthesis of the inducible enzyme quickly falls, and the concentration of the enzyme within the growing cells is reduced to a minimum, the basal level; it is maintained at this level by a basal synthesis; that is, the low level synthesis which occurs in the absence of the specific inducer. The process whereby the high induced enzyme level becomes reduced