Volume 5 of Biomembranes covers an important group of membrane proteins, the ATPases. The P-type ATPases couple the hydrolysis of ATP to the movement of ions across a membrane and are characterized by the formation of a phosphoyrlated intermediate. Included are the plasma membrane and muscle sarcoplasmic reticulum Ca 2+ -ATPases, the (Na + -K + ) -ATPase, the gastric (H + -K + ) -ATPase, the plasma membrane H + -ATPase of fungi and plants, the Mg2+ - transport ATPase, the Salmonella typhimurium, and the K + -ATPase of ...
Read More
Volume 5 of Biomembranes covers an important group of membrane proteins, the ATPases. The P-type ATPases couple the hydrolysis of ATP to the movement of ions across a membrane and are characterized by the formation of a phosphoyrlated intermediate. Included are the plasma membrane and muscle sarcoplasmic reticulum Ca 2+ -ATPases, the (Na + -K + ) -ATPase, the gastric (H + -K + ) -ATPase, the plasma membrane H + -ATPase of fungi and plants, the Mg2+ - transport ATPase, the Salmonella typhimurium, and the K + -ATPase of Escherichia coli, KdpB. The other important classes of ATPase in eukaryotic systems are the vacuolar H + -ATPases and the F0F1 ATP synthase, and, in bacteria, the anion-translocating ATPases, responsible for resistance to arsenicals and antimonials, and the (Na + -Mg 2+ ) -ATPase of Acholeplasma. Finally, eukaryotic systems contain a variety of ectonucleotidases important, for example, in hydrolysis of extracellular ATP released as a cotransmitter from cholinergic and adrenergic nerve terminals. Volume 5 of Biomembranes explores structure-function relationships for these mebrane-bound ATPases.
Read Less
Add this copy of Atpases: Volume 5 to cart. $135.75, new condition, Sold by Ingram Customer Returns Center rated 5.0 out of 5 stars, ships from NV, USA, published 1996 by Elsevier Science.
Add this copy of Atpases: Volume 5 to cart. $145.82, new condition, Sold by Ria Christie Books rated 5.0 out of 5 stars, ships from Uxbridge, MIDDLESEX, UNITED KINGDOM, published 1996 by Elsevier Science.