{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,13]],"date-time":"2025-10-13T14:59:23Z","timestamp":1760367563457},"reference-count":23,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2012,7,19]],"date-time":"2012-07-19T00:00:00Z","timestamp":1342656000000},"content-version":"vor","delay-in-days":10245,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["bpspubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["British J Pharmacology"],"published-print":{"date-parts":[[1984,7]]},"abstract":"<jats:p><jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>The cellular and subcellular distributions of adenosinetriphosphatases (ATPases) were examined in guinea\u2010pig gastric mucosal cells. All cell types displayed Mg<jats:sup>2+<\/jats:sup>\u2010ATPase and bicarbonate (HCO<jats:sub>&amp;3bar;<\/jats:sub>)\u2010stimulated ATPase activity. K<jats:sup>+<\/jats:sup>\u2010ATPase was located only in fractions derived from parietal cells.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Differential and density\u2010gradient centrifugation of material prepared from parietal cells revealed that K<jats:sup>+<\/jats:sup>\u2010ATPase activity was located in a tubulo\u2010vesicular membrane fraction. Enzyme activity was ten fold greater in this fraction than in a crude parietal cell homogenate.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The substituted benzimidazoles, omeprazole and picoprazole, inhibited K<jats:sup>+<\/jats:sup>\u2010ATPase (IC<jats:sub>50<\/jats:sub> 1.8 \u00b1 0.5 \u03bcmol 1<jats:sup>\u22121<\/jats:sup> and 3.1 \u00b1 0.4 \u03bcmol 1<jats:sup>\u22121<\/jats:sup>, respectively). Detailed kinetic analysis indicated that these compounds were non\u2010competitive and reversible inhibitors of the enzyme. In contrast cimetidine and verapamil were without effect on the enzyme.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The relevance of the inhibition of K<jats:sup>+<\/jats:sup>\u2010ATPase to the antisecretory activity of the benzimidazoles, in experimental animals and man, is discussed.<\/jats:p><\/jats:list-item>\n<\/jats:list><\/jats:p>","DOI":"10.1111\/j.1476-5381.1984.tb10803.x","type":"journal-article","created":{"date-parts":[[2012,7,20]],"date-time":"2012-07-20T16:19:30Z","timestamp":1342801170000},"page":"651-657","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["Inhibition of partially purified K\/H<sup>+<\/sup> \u2010ATPase from guinea\u2010pig isolated and enriched parietal cells by substituted benzimidazoles"],"prefix":"10.1111","volume":"82","author":[{"given":"W.","family":"Beil","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K.\u2010Fr.","family":"Sewing","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2012,7,19]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/S0021-9258(18)44883-1","article-title":"A microspec\u2010trophotometric method for the determination of cytochrome oxidase","volume":"208","author":"COOPERSTEIN S.J.","year":"1951","journal-title":"J. biol. 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