CO2 and bicarbonate exchange in the rat liver.

Several forms of carbonic anhydrase (CA) have been detected in hepatocytes. The distribution of these enzymes appears to be heterogeneous in the hepatic lobule, and the specific isoenzyme that predominates is influenced by sex steroid levels in the animal. In the present study, experiments were conducted in isolated male rat livers perfused with erythrocyte-free solutions, which were devoid of CA to see if there were sufficient tissue CA activity accessible to the plasma to ensure equilibration between labeled HCO3- and CO2 during a single passage from the portal vein to the hepatic vein. After injection of H14CO3- into the portal vein, emergence of the 14C label from the hepatic vein was slightly more rapid than after injections of 14CO2. After infusion of 5-250 microM of acetazolamide, an inhibitor of CA, H14CO3- was virtually confined to the extracellular space during a single transit through the organ, whereas the outflow of 14CO2 was very prolonged, suggesting that some of the 14C had been "trapped" within the hepatic cells as H14CO3-. Inhibition of CA activity in the intact organ with low doses of acetazolamide suggests the presence of a readily inhibitable isoenzyme of CA on the surface of the hepatocytes, which is directly accessible to both HCO3- and acetazolamide. The outflow patterns of 14CO2 and H14CO3- became the same after infusion of erythrocyte CA into the portal vein. On the basis of the pH of the perfusate and the cellular distribution of 14CO2 and H14CO3- in the presence of CA, an intracellular pH value of 7.26 was calculated.(ABSTRACT TRUNCATED AT 250 WORDS)