[Distribution of carbonic anhydrase, K+-ATPase and K+-phosphatase in subcellular fractions of gastric mucosa].
The distribution of carbonic anhydrase, K+-ATPase and K+-phosphatase in the subcellular fractions of gastric mucosa was studied. It was found that 90% of carbonic anhydrase are localized in the hyaloplasm, whereas K+-ATPase and K+-phosphatase are predominantly localized in the microsomal fraction. Subfractionation of the microsomal fraction in a sucrose density gradient showed that the membrane-bound carbonic anhydrase (5% of total content) and K+-ATPase are bound to various cell organelles. It is concluded that carbonic anhydrase functions as an intracellular pH-stat and is not directly involved in proton generation by the cell.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002256:Carbonic Anhydrases / Q000032:analysis*; D002458:Cell Fractionation; D005753:Gastric Mucosa / Q000201:enzymology*; D008297:Male; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011188:Potassium / Q000378:metabolism; D011817:Rabbits; D013347:Subcellular Fractions / Q000201:enzymology
D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D002256:Carbonic Anhydrases; D011188:Potassium
Raspredelenie karboangidrazy, K-ATPazy I K-fosfatazy v subkletochnykh fraktsiiakh slizistoĭ obolochki zheludka.