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Registro Completo |
Biblioteca(s): |
Ebooks. |
Data corrente: |
15/08/2008 |
Data da última atualização: |
16/06/2011 |
Autoria: |
LEE, A. G. |
Afiliação: |
A. G. Lee. |
Título: |
ATPases |
Ano de publicação: |
1996 |
Fonte/Imprenta: |
Greenwich, Conn. : JAI Press, c1996. |
Páginas: |
xii, 428 p. |
Descrição Física: |
ill. ;24 cm. |
Série: |
Biomembranes ; |
ISBN: |
9781559386623 |
Idioma: |
Inglês |
Conteúdo: |
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. |
Categoria do assunto: |
-- |
URL: |
https://www.sciencedirect.com/science/publication?issn=18745342&volume=5
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Marc: |
LEADER 01669nam a2200145 a 4500 001 1711172 005 2011-06-16 008 1996 bl uuuu u0uu1 u #d 020 $a9781559386623 100 1 $aLEE, A. G. 245 $aATPases$h[electronic resource] 260 $aGreenwich, Conn. : JAI Press$c1996 300 $axii, 428 p. $cill. ;24 cm. 490 $aBiomembranes ; 520 $aVolume 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<SUP>2+</SUP> -ATPases, the (Na<SUP>+</SUP> -K<SUP>+</SUP>) -ATPase, the gastric (H<SUP>+</SUP> -K<SUP>+</SUP>) -ATPase, the plasma membrane H<SUP>+</SUP> -ATPase of fungi and plants, the Mg2+ - transport ATPase, the Salmonella typhimurium, and the K<SUP>+</SUP> -ATPase of Escherichia coli, KdpB. The other important classes of ATPase in eukaryotic systems are the vacuolar H<SUP>+ </SUP>-ATPases and the F0F1 ATP synthase, and, in bacteria, the anion-translocating ATPases, responsible for resistance to arsenicals and antimonials, and the (Na<SUP>+</SUP> -Mg<SUP>2+</SUP>) -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.
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3. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | ANGUS, A. A.; LEE, A.; LUM, M. R.; SHEHAYEB, M.; HESSABI, R.; FUJISHIGE, N. A.; YERRAPRAGADA, S.; KANO, S.; SONG, N.; YANG, P.; SANTOS, P. E. de los; FARIA, S. M. de; DAKORA, F. D.; WEINSTOCK, G.; HIRSCH, A. M. Nodulation and effective nitrogen fixation of Macroptilium atropurpureum (siratro) by Burkohlderia tuberum, a nodulating and plant growth promoting beta-proteobacterium, are influenced by environmental factors. Plant Soil Online, 26 jun., 2013Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
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