Studies on the localization and properties of rat duodenal HCO3--ATPase with special relation to alkaline phosphatase.
Brush-border membrane fractions were isolated from rat duodenum. Purity and integrity of the fraction was confirmed by electron microscopy, enzymic analysis and demonstration of Na+-dependent glucose uptake. The membranes were enriched 15-fold in alkaline phosphatase and alpha-glucosidase and 6-fold in HCO3--ATPase activities. Assays of latent activity indicated that these enzymes were predominantly localised to the external aspect of the microvillus membrane. The enzymes were solubilised and subjected to analysis by gel filtration, ion exchange and phenylboronate chromatography. No separation of alkaline phosphatase and HCO3--ATPase was obtained and it is suggested that they reflect the same enzyme activity. The apparent activation by HCO3- was investigated, and was found to be due to shifts in the pH dependency of the activity due to changes in ionic strength.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D027321:Anion Transport Proteins; D002458:Cell Fractionation; D004386:Duodenum / Q000201:enzymology*; D007413:Intestinal Mucosa / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D008871:Microvilli / Q000201:enzymology* / Q000648:ultrastructure; D051381:Rats; D011919:Rats, Inbred Strains
D027321:Anion Transport Proteins; D000469:Alkaline Phosphatase; D000251:Adenosine Triphosphatases; C031652:anion-sensitive ATPases