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Primary Active Transport

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 Transport

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...

ATP Driven Pumps I: An Overview

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...

ATP Driven Pumps III: V-type Pumps

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 Pumps

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...

Regulation of Sodium and Potassium

Regulation of Sodium and Potassium

The regulation of sodium and potassium ion concentrations in the human body is a complex process governed primarily by hormones such as aldosterone, antidiuretic hormone (ADH), and atrial natriuretic peptide (ANP).
Sodium Regulation
Sodium ions make up approximately 90% of extracellular cations, with a normal blood plasma concentration of 136–148 mEq/L. A decrease in blood volume and pressure triggers the release of renin from granular cells in the juxtaglomerular complex (JGC), primarily in...

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Related Experiment Video

Updated: Jun 6, 2026

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

Proton diet for the sodium pump.

Hans-Jürgen Apell¹, Gabriela Benz, Daniel Sauerbrunn

¹Department of Biology, University of Konstanz, 78464 Konstanz, Germany. h-j.apell@uni-konstanz.de

|December 15, 2010

Summary

This summary is machine-generated.

The sodium-potassium pump (Na,K-ATPase) can transport protons (H+) in an electroneutral manner when Na+ and K+ ions are absent. This H+-only mode, with a 2 H+/2 H+/1 ATP stoichiometry, operates independently of the pump

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

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Published on: March 30, 2015

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Published on: February 3, 2018

Area of Science:

Biochemistry
Molecular Biology
Membrane Transport

Background:

The Na,K-ATPase is a crucial ion transporter in cell physiology.
Its activity is typically dependent on sodium (Na+) and potassium (K+) ions.
Under non-physiological conditions, alternative transport mechanisms may emerge.

Purpose of the Study:

To investigate the functional properties of Na,K-ATPase in the absence of Na+ and K+ ions.
To elucidate the mechanism of pH-dependent ATP hydrolysis and ion transport.
To determine the stoichiometry and directionality of ion movement.

Main Methods:

Experiments using reconstituted proteoliposomes to study Na,K-ATPase.
pH-dependent ATP hydrolysis assays.
Ouabain inhibition studies.
Time-resolved ATP-concentration jump experiments.

Main Results:

Na,K-ATPase exhibits pH-dependent ATP hydrolysis in the absence of Na+ and K+.
This activity, inhibited by ouabain, represents an H+-only transport mode.
Electroneutral transport with a stoichiometry of 2 H+/2 H+/1 ATP was demonstrated.
Protons (H+) do not occupy the Na+-specific binding site.

Conclusions:

A modified Post-Albers pump cycle explains the observed H+-only transport.
H+ ions act as congeners for Na+ and K+ under specific conditions.
This study reveals a novel functional mode of the Na,K-ATPase.