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Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
Active Transport01:14

Active Transport

Active transport is a critical biological process that allows cells to move solutes against an electrochemical gradient. This process requires direct energy input and is characterized by its selectivity, saturability, and susceptibility to competitive inhibition.
Primary active transporters, like Na+, K+ and -ATPase, directly utilize ATP to move ions across the membrane. These transporters play significant roles in various physiological processes. For instance, Na+, K+ and -ATPase maintain...
Primary Active Transport01:29

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would not...
Primary Active Transport01:47

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they...

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Related Experiment Video

Updated: Jun 11, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

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

The renal H,K-ATPases.

Megan M Greenlee1, Irma Jeanette Lynch, Michelle L Gumz

  • 1Research Service, North Florida/South Georgia Veterans Health System, USA.

Current Opinion in Nephrology and Hypertension
|July 10, 2010
PubMed
Summary

Hydrogen potassium adenosine triphosphatases (H,K-ATPases) are crucial for physiological function. Recent evidence shows both gastric (HKalpha1) and nongastric (HKalpha2) isoforms play roles in acid-base and sodium balance, even in normal diets.

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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Related Experiment Videos

Last Updated: Jun 11, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

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

Use of Enzymatic Biosensors to Quantify Endogenous ATP or H2O2 in the Kidney
10:00

Use of Enzymatic Biosensors to Quantify Endogenous ATP or H2O2 in the Kidney

Published on: October 12, 2015

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

Area of Science:

  • Physiology
  • Molecular Biology
  • Renal Function

Background:

  • Hydrogen potassium adenosine triphosphatases (H,K-ATPases) are membrane transport proteins.
  • Gastric (HKalpha1) and nongastric (HKalpha2) isoforms have distinct physiological roles.
  • Previous research focused on potassium (K) conservation during K depletion.

Purpose of the Study:

  • To integrate recent evidence on the physiological importance of H,K-ATPases.
  • To examine the role of H,K-ATPases in potassium (K), sodium (Na), and acid-base balance.
  • To explore the function of both isoforms in normal and K-depleted states.

Main Methods:

  • Review of recent scientific literature and evidence.
  • Analysis of findings from studies on H,K-ATPase isoforms.
  • Examination of data from HKalpha2-null mice and heterologous expression systems.

Main Results:

  • Both H,K-ATPase isoforms are active in physiological conditions, not solely during K depletion.
  • Recent findings indicate H,K-ATPases contribute to acid secretion in animals on normal diets.
  • The nongastric HKalpha2 isoform exhibits Na affinity, suggesting a role in Na balance, potentially impacting renal function.

Conclusions:

  • H,K-ATPase isoforms are active in normal physiological states.
  • The renal HKalpha2-containing H,K-ATPase may influence sodium balance.
  • These findings have significant clinical implications for understanding kidney function and H,K-ATPases in humans.