Download PDF by A.G. Lee (Eds.): ATPases

By A.G. Lee (Eds.)

ISBN-10: 1559386622

ISBN-13: 9781559386623

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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Biochim. Biophys. Acta 897, 207-216. , & Baumert, H. G. (1993). Identification of a cross-linked double-peptide from the catalytic site of the Ca "^-ATPase of sarcoplasmic reticulum formed by the Ca ^- and pH-dependent reaction with ATP y-P-imidazolidate. FEBS Lett. 324, 314-318. , & Champeil, P. (1992). The metal sites on sarcoplasmic reticulum membranes that bind lanthanide ions with the highest affinity are not the ATPase Ca transport sites. J. Biol. Chem. 267, 10302-10312. Henderson, I. M. , Khan, M.

Modyanov, N. N. (1988). In: The Na,K-Pump, Part A: Molecular Aspects (Skou, J. C, Norby, J. , Maunsbach, A. ) pp. 181—188. Alan R. Liss, New York. East, J. , Tunwell, R. E. , Mata, A. , & Lee, A. G. (1992). Studies of the structure and function of sarcoplasmic reticulum (Ca "^-Mg "^)-ATPase using immunological approaches. Biochem. Soc. Trans. 20, 550-554. , & Dani, J. A. (1987). An introduction to molecular architecture and permeability of ion channels. Ann. Rev. Biophys. Chem. 16, 205—226.

Chem. 260, 14421-14423. Seebregts, C. , & Mcintosh, D. B. (1989). 2',3'-0-(2,4,6-trinitrophenyl)-8-azido-adenosine mono-, di-, and triphosphates as photoaflfmity probes of the Ca ^-ATPase of sarcoplasmic reticulum. Regulatory/superfluorescent nucleotides label the catalytic site with high efficiency. J. Biol. Chem. 264, 2043-2052. , & Portillo, F. (1990). Catalytic and regulatory sites of yeast plasma membrane H -ATPase studied by directed mutagenesis. Biochim. Biophys. Acta 1018, 195-199. Skerjanc, I.

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