Abstract
Carbonic anhydrase activity was studied in stomach and kidney homogenates, and isoenzymes were purified from erythrocytes and livers of male and female rats. Two liver isoenzymes of male and female rats and one erythrocyte isoenzyme had low CO 2 hydration activity. The enzymes of stomach and kidney, one isoenzyme of erythrocytes and one of female rat liver had high CO 2 hydration activity. The esterase activity toward p-nitrophenyl acetate paralleled the CO 2 hydration activity of all the isoenzymes. However, the esterase activity toward β-naphthyl acetate was either absent or did not show any correlation with the CO 2 hydration activity of isoenzymes. Male rat liver carbonic anhydrases were 1000 times less sensitive to sulfonamides than female rat liver carbonic anhydrases for the inhibition both of CO 2 hydration and esterase activity. Male rat liver carbonic anhydrases were as sensitive to inhibition by monovalent anions as were the female rat liver carbonic anhydrases. It is concluded that the active site of carbonic anhydrases from male rat liver is more hydrophilic than the active site of carbonic anhydrase from female rat liver or other tissues of the rat.
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