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Related Concept Videos

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...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
ATP Synthase: Mechanism01:48

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
ATP Driven Pumps III: V-type Pumps01:30

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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...

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

Elfrieda Fodor1, Natalya U Fedosova, Csilla Ferencz

  • 1Institute of Biophysics, Biological Research Centre, Szeged, Hungary.

Biochimica Et Biophysica Acta
|January 12, 2008
PubMed
Summary
This summary is machine-generated.

Ions protect Na,K-ATPase enzymes from shark and pig kidney against rapid inactivation and thermal denaturation. Millimolar cations stabilize these vital ion pumps through distinct mechanisms, correlating with their physiological roles.

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Published on: October 9, 2021

Area of Science:

  • Biochemistry
  • Enzyme kinetics
  • Protein thermostability

Background:

  • Na,K-ATPase is crucial for ion transport in animal cells.
  • Enzyme stability is influenced by environmental factors like ions and temperature.
  • Comparative studies of Na,K-ATPase from different species can reveal functional adaptations.

Purpose of the Study:

  • To investigate the effect of ions on the thermostability and unfolding of Na,K-ATPase from shark salt gland and pig kidney.
  • To compare the stabilization mechanisms of ions on these two enzymes.
  • To correlate enzyme stability with physiological conditions.

Main Methods:

  • Differential scanning calorimetry (DSC) to assess thermal unfolding and stability.
  • Activity assays to measure enzyme inactivation rates.
  • Comparative analysis of shark and pig kidney Na,K-ATPase.

Main Results:

  • Shark Na,K-ATPase is less thermostable than pig kidney Na,K-ATPase.
  • Increasing ionic strength with histidine, NaCl, or KCl protects both enzymes against inactivation.
  • Cations stabilize Na,K-ATPase through at least two distinct mechanisms, affecting different cooperative domains.

Conclusions:

  • The differential thermostability of shark and pig kidney Na,K-ATPases correlates with their physiological temperatures.
  • Millimolar concentrations of cations provide significant stabilization to Na,K-ATPase.
  • Lipid environment likely contributes to the observed differences in enzyme stability.