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THE INTERACTION OF K + WITH GASTRIC PARIETAL CELLS AND GASTRIC ATPASE *
Author(s) -
Sachs G.,
Berglindh T.,
Rabon E.,
Wallmark B.,
Barcellona M. L.,
Stewart H. B.,
Saccomani G.
Publication year - 1980
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1980.tb15391.x
Subject(s) - parietal cell , secretion , cytoplasm , enzyme , atpase , chemistry , gastric chief cell , vesicle , gastric acid , reagent , biochemistry , gastric secretion , cell , biophysics , gastric mucosa , stomach , biology , membrane
The gastric H+ secretion in isolated cell requires K+ and is ATP dependent. There is also evidence in the cell system for Na+ inhibition of H+ secretion. The isolated gastric ATPase also shows K+ activation and inhibition by K+ or Na+ located on the ATP binding side of the enzyme, which corresponds to the cytoplasmic face of the enzyme. Gastric vesicles are activated in terms of transport activity by internal K+, and this site, inhibited by reagents that modify carboxyl groups, is required for enzyme turnover and transport.