Mg2+-HCO-3-ATPase and carbonic anhydrase in rat intestinal mucosa.
Mg2+-dependent and HCO-3-stimulated ATPase activity was highest in the brush border (microvilli) of rat duodenal mucosa compared with that of the other gastrointestinal mucosa. This ATPase may be useful to neutralize the gastric acid in the duodenal lumen. Carbonic anhydrase seems to accomplish a subsidiary role in the above reaction.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase; D002256:Carbonic Anhydrases / Q000378:metabolism*; D005753:Gastric Mucosa / Q000201:enzymology*; D007413:Intestinal Mucosa / Q000201:enzymology*; D007420:Intestine, Large / Q000201:enzymology; D007421:Intestine, Small / Q000201:enzymology; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D014018:Tissue Distribution
D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; C032666:magnesium-bicarbonate ATPase; D002256:Carbonic Anhydrases