Abstract
Indomethacin showed a dose-, time-, and pH-dependent, noncompetitive inhibitory effect on hog gastric H+/K(+)-ATPase. Four percent of total indomethacin in the buffer (0.20 mmol/liter) bound to the H+/K(+)-ATPase vesicles (15 micrograms/ml). It markedly quenched the intrinsic fluorescence of the enzyme, and decreased the membrane fluidity. Thus, the inhibitor effect of indomethacin may arise from both a direct effect on the hydrolytic and H+ transport functions of the enzyme and a disturbing effect on the lipid bilayer of the vesicle.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / antagonists & inhibitors
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Adenosine Triphosphatases / metabolism
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Animals
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Cell Membrane / drug effects
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Fluorescence
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Gastric Mucosa / drug effects
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Gastric Mucosa / enzymology*
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Gastric Mucosa / ultrastructure
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H(+)-K(+)-Exchanging ATPase / metabolism
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Hydrogen-Ion Concentration
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Indomethacin / pharmacology*
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Kinetics
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Lipid Bilayers / metabolism*
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Proton Pump Inhibitors*
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Proton Pumps
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Swine
Substances
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Lipid Bilayers
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Proton Pump Inhibitors
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Proton Pumps
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Adenosine Triphosphatases
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H(+)-K(+)-Exchanging ATPase
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Indomethacin