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Description
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 Ca2+ -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+ -Mg2+) -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.
Table of Contents
Contents. List of Contributors. Preface. Structure of the SR/ER Ca2+-ATPase (A.G. Lee). Kinetic Characterization of Sarcoplasmic Reticulum Ca2+-ATPase (P. Champeil). Cardiac Ca2+-ATPase and Phopholamban (A.G. Lee). The Calcium Pump of Plasma Membranes (J. Krebs and D. Guerini). The Sodium Pump (F. Cornelius). The Gastric H+/K+-ATPase (J.M. Shin, D. Bayle, K. Bamberg, and G. Sachs). The Plasma Membrane H+-ATPase of Fungi and Plants (F. Portillo, P. Eraso, and R. Serrano). Anion-Translocating ATPases (B.P. Rosen, S. Dey, and D. Dou). The Magnesium Transport ATPases of Salmonella Typhimurium (T. Tao and M.E. Maguire). The Acholeplasma Laidlawii Na2+Mg2-ATPase (R.N. McElhaney). Vacuolar H+-ATPase (N. Nelson). The F0 F1 ATP Synthase: Structures Involved in Catalysis, Transport, and Coupling (R.K. Nakamoto and M. Futai). ATP-Diphophohydrolases, Apyrases, and Nucleotide Phosphohydrolases: Biochemical Properties and Functions (A.R. Beaudoin, J. Sevigny, and M. Picher). The KDP-ATPase of Escherichia Coli (K. Altendorf and W. Epstein). Index.
Details
- No. of pages:
- 428
- Language:
- English
- Copyright:
- © 1996
- Published:
- 17th December 1996
- Imprint:
- Elsevier Science
- eBook ISBN:
- 9780080527703
- Print ISBN:
- 9781559386623
- Print ISBN:
- 9780444546555
About the editor
A.G. Lee
Affiliations and Expertise
Department of Biochemistry, University of Southampton, Southampton, England
Reviews
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 Ca2+ -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+ -Mg2+) -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.