Independent Genetic Control of the Catalytic Activity and the Rate of Degradation of Catalase in Mice

Abstract

An examination of three inbred strains of mice differing with respect to liver and kidney catalase activity reveals two distinct genetic factors controlling the level of liver catalase activity. The first genetic factor controls the catalytic activity of the enzyme. Specific activity of purified enzyme from C57BL/6 and C57BL/Ha strains is 60% that of the DBA/2 strain. The second factor controls the content of liver catalase. Liver catalase of CS7BL/Ha is degraded in vivo at a rate one-half that of liver catalase of DBA/2 and C57BL/6, resulting in the accumulation of twice as many catalase molecules in C57BL/Ha. The factor affecting turnover of catalase is apparently specific for catalase of liver since no differences exist in kidney catalase levels between C57BL/Ha and C57BL/6. Furthermore, this factor does not appear to alter the metabolism of peroxisomes or of liver protein since no substantial differences are observed among the strains with respect to liver urate oxidase activity levels and the turnover rate of liver protein. It is particularly significant that the genetic factor affecting the amount of liver catalase does so by altering the rate of catalase degradation rather than the rate of synthesis, confirming the previously published report of Rechcigl and Heston (Biochem. Biophys. Res. Commun., 27, 119 (1967)). Thus, these studies emphasize that the quantity of an enzyme in animal cells is a balance between the rate of synthesis and the rate of degradation of the enzyme.