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The sodium–potassium pump (sodium–potassium adenosine triphosphatase, also known as Na + /K +-ATPase, Na + /K + pump, or sodium–potassium ATPase) is an enzyme (an electrogenic transmembrane ATPase) found in the membrane of all animal cells. It performs several functions in cell physiology.
The sodium–potassium pump is a critical enzyme for regulating sodium and potassium levels in cells. Potassium is the main intracellular ion for all types of cells, while having a major role in maintenance of fluid and electrolyte balance. [1] [2] Potassium is necessary for the function of all living cells and is thus present in all plant and ...
Sick cell syndrome is a medical condition characterised by reduced functioning of the cellular Na+/K+ pump, [1] which is responsible for maintaining the internal ion homeostasis. The clinical result is a rise in blood K+ level and drop of blood Na+ levels
At the resting voltage potential, a pump is pumping 2 K+ ions into the cell, and pumps 3 Na+ ions out of the cell. Since this is a nett electrical current, it makes the cell's membrane voltage slightly more negative. This causes a passive influx of 1 K+ ion, driven by the membrane voltage.
Membrane potential is maintained principally by the concentration gradient and membrane permeability to potassium with some contribution from the Na+/K+ pump. The potassium gradient is critically important for many physiological processes, including maintenance of cellular membrane potential , homeostasis of cell volume, and transmission of ...
The sodium–potassium pump, a critical enzyme for regulating sodium and potassium levels in cells. Sodium ions (Na +) are necessary in small amounts for some types of plants, [1] but sodium as a nutrient is more generally needed in larger amounts [1] by animals, due to their use of it for generation of nerve impulses and for maintenance of electrolyte balance and fluid balance.
The P-type ATPases, also known as E 1-E 2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. [1] P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation (hence P) of a key conserved aspartate residue within the pump and their energy source ...
11928 Ensembl ENSG00000163399 ENSMUSG00000033161 UniProt P05023 Q5TC02 Q8VDN2 RefSeq (mRNA) NM_000701 NM_001001586 NM_001160233 NM_001160234 NM_144900 RefSeq (protein) NP_000692 NP_001153705 NP_001153706 NP_659149 Location (UCSC) Chr 1: 116.37 – 116.41 Mb Chr 3: 101.48 – 101.51 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein domain Gastric H + /K + -ATPase, N terminal ...