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Inhibition of the gastric (H+ + K+)-ATPase by fenoctimine

Biochemical Pharmacology

Jul 1, 1985

W W ReenstraJ G Forte

Abstract

The effects of fenoctimine, an inhibitor of gastric acid secretion, on the microsomal (H+ + K+)-ATPase were studied. In the micromolar concentration range, fenoctimine inhibited hydrolysis of ATP and p-nitrophenyl phosphate by the (H+ + K+)-ATPase. Inhibition was reversible and noncompe...read more

Mentioned in this Paper

Microsomal Membrane
Anti-Ulcer Agent
Tissue Membrane
Adenosine Triphosphatases
Structure of Pyloric Gland
Piperidines
4-nitrophenylphosphate
H(+)-K(+)-Exchanging ATPase
Metabolic Inhibition
Turbidity Measurement
Paper Details
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Inhibition of the gastric (H+ + K+)-ATPase by fenoctimine

Biochemical Pharmacology

Jul 1, 1985

W W ReenstraJ G Forte

PMID: 2990481

DOI: 10.1016/0006-2952(85)90790-7

Abstract

The effects of fenoctimine, an inhibitor of gastric acid secretion, on the microsomal (H+ + K+)-ATPase were studied. In the micromolar concentration range, fenoctimine inhibited hydrolysis of ATP and p-nitrophenyl phosphate by the (H+ + K+)-ATPase. Inhibition was reversible and noncompe...read more

Mentioned in this Paper

Microsomal Membrane
Anti-Ulcer Agent
Tissue Membrane
Adenosine Triphosphatases
Structure of Pyloric Gland
Piperidines
4-nitrophenylphosphate
H(+)-K(+)-Exchanging ATPase
Metabolic Inhibition
Turbidity Measurement

Similar Papers Found In These Feeds

ATP Synthases

ATP synthases are enzymes located in the inner mitochondrial membrane that catalyze the synthesis of ATP during cellular respiration. Discover the latest research on ATP synthases here.

Related Papers

Paper Details
References
  • References1
  • Citations1
1
  • References1
  • Citations1
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