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Characterization of Syrian hamster gastric mucosal H+,K+-ATPase

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Abstract

Employing a simple one-step sucrose gradient fractionation method, gastric mucosal membrane of Syrian hamster was prepared and demonstrated to be specifically enriched in H+,K+-ATPase activity. The preparation is practically devoid of other ATP hydrolyzing activity and contains high K+-stimulated ATPase, activity of at least 4–5 fold compared to basal ATPase activity. The H+,K+-ATPase showed hydroxylamine-sensitive phosphorylation and K+-dependent dephosphorylation of the phospho-enzyme, characteristic inhibition by vanadate, omeprazole and SCH 28080, and nigericin-reversible K+-dependent H+-transport — properties characteristic of gastric proton pump One notable difference with H+,K+-ATPase of other species has been the observation of valinomycin-independent H+ transport in such membrane vesicles. It is proposed that such H+,K+-ATPase-rich hamster gastric mucosal membrane preparation might provide a unique model to study physiological aspects of H+,K+-ATPase-function in relation to HCl secretion.

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Chatterjee, P.K., Das, P.K. Characterization of Syrian hamster gastric mucosal H+,K+-ATPase. Mol Cell Biochem 148, 95–103 (1995). https://doi.org/10.1007/BF00928146

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