By A.G. Lee (Eds.)
Quantity five of Biomembranes covers a tremendous staff of membrane proteins, the ATPases. The P-type ATPases couple the hydrolysis of ATP to the circulation of ions throughout a membrane and are characterised through the formation of a phosphoyrlated intermediate. incorporated are the plasma membrane and muscle sarcoplasmic reticulum Ca2+ -ATPases, the (Na+ -K+) -ATPase, the gastric (H+ -K+) -ATPase, the plasma membrane H+ -ATPase of fungi and vegetation, the Mg2+ - delivery ATPase, the Salmonella typhimurium, and the K+ -ATPase of Escherichia coli, KdpB. the opposite very important periods of ATPase in eukaryotic structures are the vacuolar H+ -ATPases and the F0F1 ATP synthase, and, in micro organism, the anion-translocating ATPases, liable for resistance to arsenicals and antimonials, and the (Na+ -Mg2+) -ATPase of Acholeplasma. eventually, eukaryotic platforms comprise a number of ectonucleotidases vital, for instance, in hydrolysis of extracellular ATP published as a cotransmitter from cholinergic and adrenergic nerve terminals. quantity five of Biomembranes explores structure-function relationships for those mebrane-bound ATPases.
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Additional resources for ATPases
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ATPases by A.G. Lee (Eds.)