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Related Experiment Video

Updated: May 10, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

Gastric H+,K+-ATPase.

Jai Moo Shin¹, Keith Munson, George Sachs

¹Department of Physiology and Medicine, University of California at Los Angeles, and VA Greater Los Angeles Healthcare System, Los Angeles, California, USA. jaishin@ucla.edu

Comprehensive Physiology

|June 5, 2013

Summary

The gastric H(+),K(+)-ATPase, crucial for acid secretion, has its structure elucidated through modeling and mutagenesis. Inhibitors help refine understanding of its proton pump mechanism and luminal vestibule.

Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

The gastric H(+),K(+)-ATPase is the primary enzyme responsible for gastric acid secretion.
This enzyme comprises a catalytic α subunit and a structural β subunit, essential for its function.

Purpose of the Study:

To elucidate the three-dimensional structure and mechanism of the gastric H(+),K(+)-ATPase.
To investigate the binding sites and mechanisms of action of various inhibitors targeting this enzyme.

Main Methods:

Homology modeling and site-directed mutagenesis were employed to determine the enzyme's structure.
Analysis of luminal inhibitors, including acid-activated covalent and K(+)-competitive types, aided in structural refinement and functional studies.

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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Functional Characterization of Na⁺/H⁺ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Related Experiment Videos

Last Updated: May 10, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Functional Characterization of Na⁺/H⁺ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Main Results:

A model for proton extrusion and potassium reabsorption was established, identifying key amino acid residues and binding sites.
Inhibitor studies facilitated the identification of all ten transmembrane segments and provided insights into the luminal vestibule structure.

Conclusions:

The study provides a detailed structural and mechanistic understanding of the gastric H(+),K(+)-ATPase.
Insights gained are crucial for the development of novel therapeutic agents for acid-related gastrointestinal diseases.