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CO2 and bicarbonate exchange in the rat liver

CO2 and bicarbonate exchange in the rat liver LIPSEN, BRYAN, AND RICHARD M. EFFROS. bicarbonate the liver. J. Appl. Physiol. 65(6): 2736- 2743, 1988.-Several forms of carbonic anhydrase (CA) have beendetected hepatocytes.The distribution of theseenzymes appears to be heterogeneous the hepatic lobule, and the specific isoenzymethat predomatesis fluenced by sex steroid levels the animal. the present study, experiments were conducted isolated male perfusedwith erythrocyte-free solutions, which were devoid of CA to seeif there were sufficient tissue CA activity accessible the plasma to to ensure equilibion between labeled HCO; and COZdurg a sgle passage from the portal ve to the hepatic ve. After jection of H14CO; to the portal ve, emergence the 14C of label from the hepatic ve was slightly more rapid than after jections of 14C02.After fusion of 5-250 PM of acetazolamide, an hibitor of CA, H14C0; was virtually confed to the extracellular space durg a sgle transit through the organ, whereasthe outflow of 14C02 was very prolonged, suggestg that some of the 14Chad been “trapped” with the hepatic cells asH14C0;. hibition of CA activity the tact organ with low doses acetazolamidesuggests presenceof of the a readily hibitable isoenzyme of CA on the surface of the hepatocytes, which is directly accessibleto both HCO: and acetazolamide. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Applied Physiology The American Physiological Society

CO2 and bicarbonate exchange in the rat liver

Journal of Applied Physiology , Volume 65: 2736 – Dec 1, 1988

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Publisher
The American Physiological Society
Copyright
Copyright © 1988 the American Physiological Society
ISSN
8750-7587
eISSN
1522-1601
Publisher site
See Article on Publisher Site

Abstract

LIPSEN, BRYAN, AND RICHARD M. EFFROS. bicarbonate the liver. J. Appl. Physiol. 65(6): 2736- 2743, 1988.-Several forms of carbonic anhydrase (CA) have beendetected hepatocytes.The distribution of theseenzymes appears to be heterogeneous the hepatic lobule, and the specific isoenzymethat predomatesis fluenced by sex steroid levels the animal. the present study, experiments were conducted isolated male perfusedwith erythrocyte-free solutions, which were devoid of CA to seeif there were sufficient tissue CA activity accessible the plasma to to ensure equilibion between labeled HCO; and COZdurg a sgle passage from the portal ve to the hepatic ve. After jection of H14CO; to the portal ve, emergence the 14C of label from the hepatic ve was slightly more rapid than after jections of 14C02.After fusion of 5-250 PM of acetazolamide, an hibitor of CA, H14C0; was virtually confed to the extracellular space durg a sgle transit through the organ, whereasthe outflow of 14C02 was very prolonged, suggestg that some of the 14Chad been “trapped” with the hepatic cells asH14C0;. hibition of CA activity the tact organ with low doses acetazolamidesuggests presenceof of the a readily hibitable isoenzyme of CA on the surface of the hepatocytes, which is directly accessibleto both HCO: and acetazolamide.

Journal

Journal of Applied PhysiologyThe American Physiological Society

Published: Dec 1, 1988

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