This paper examines the activity and importance of sodium pumps to the body.
Written in 2007; 1,387 words; 11 sources; MLA; $ 46.95
Paper Summary:
In this article, the writer explains that the Na+-K+-ATPase (Sodium Pump)The Na+-K+-ATPase, or sodium pump is a highly-conserved integral membrane protein existing in almost all cells in higher organisms. The writer further explains that a human at rest contains cells that consist roughly of 25% cytoplasmic ATP which is hydrolyzed by sodium pumps. Approximately 70% of ATP is consumed to fuel sodium pumps in nerve cells. In the body, the autonomic nervous system heart cells are regulated through these receptors to modulate certain ion-kinetic structures to influence ion movement. The writer concludes that the sodium pump is involved in cell junction maintenance, thus ensuring that the heart cells stay connected with one another. The writer also notes that without this sodium pump, the body cannot function and the heart never develops.
From the Paper:
"Description of the structure of this molecule is still uncertain, but information is available to define the amino acids involved in ATP and cation binding. The sodium pump, which is located within the outside membrane of the cell, grabs sodium and releases it on the other side of the membrane, repositioning itself to do so, then grabs potassium and releases it within the cell: Within the cell, ATP is bound to the empty pump, the N/A+ ions approach the pump, are bound to the pump until the pump is loaded with (3) Na+ ions, ATP is hydrolyzed, the pump phosphorylated, the pump reorients in the membrane and the Na+ ions start to fall off outside of the cell. As the Na+ ions are released, (2) K+ ions approach the pump, are bound and dephosporylation takes place. The ATP is bound to the pump, a conformational change takes place when the K+ is in the cell and they are delivered into the interior of the cell and the pump is ready to start again. Although it is difficult to explain the structure of this "pump," based on primary amino acid sequence, it probably possesses 8 or 10 transmembrane domains."
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