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Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, Sajal Chakraborti; Naranjan S Dhalla


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Автор: Sajal Chakraborti; Naranjan S Dhalla
Название:  Regulation of Ca2+-ATPases,V-ATPases and F-ATPases
ISBN: 9783319247786
Издательство: Springer
Классификация:


ISBN-10: 3319247786
Обложка/Формат: Hardcover
Страницы: 586
Вес: 1.06 кг.
Дата издания: 16.12.2015
Серия: Advances in Biochemistry in Health and Disease
Язык: English
Издание: 1st ed. 2016
Иллюстрации: 71 tables, color; 4 tables, black and white; 26 illustrations, color; 75 illustrations, black and white; xiii, 586 p. 101 illus., 26 illus. in color.
Размер: 234 x 156 x 33
Читательская аудитория: Professional & vocational
Основная тема: Protein Structure
Ссылка на Издательство: Link
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Поставляется из: Германии
Описание: The three main types of the ion pump ATPase family are: (i) P-type ATPases that transport different ions across membranes and Ca2+ATPases belongs to this catagory (ii) F-type ATPase in mitochondria, chloroplasts and bacterial plasma membranes produce ATP using the proton gradient;


Regulation of Membrane Na+-K+ ATPase

Автор: Sajal Chakraborti; Naranjan S Dhalla
Название: Regulation of Membrane Na+-K+ ATPase
ISBN: 3319247484 ISBN-13(EAN): 9783319247489
Издательство: Springer
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Цена: 27950.00 р.
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Описание: Na+-K+ ATPase or Na-pump ATPase, a member of “P”-type ATPase superfamily, is characterized by association of multiple isoforms mainly of it’s ?- and ?- subunits. At present four different ?- (?-1,?-2,?-3 and ?-4) and three ?- (?-1, ?-2, and ?-3) isoforms have been identified in mammalian cells and their differential expressions are tissue specific. Regulation of Na+-K+ ATPase activity is an important but a complex process, which involves short-term and long-term mechanisms. Short-term regulation of Na+-K+ ATPase is either mediated by changes in intracellular Na+ concentrations that directly affect the Na+-pump activity or by phosphorylation/dephosphorylation-mediated by some stimulants leading to changes in its expression and transport properties. On the other hand, long-term regulation of Na+-K+ ATPase is mediated by hormones, such as mineralocorticoids and thyroid hormones, which cause changes in the transcription of genes of ?- and ?- subunits leading to an increased expression in the level of Na+-pump. Several studies have revealed a relatively new type of regulation that involves the association of small, single span membrane proteins with this enzyme. These proteins belong to the FXYD family, the members of which share a common signature sequence encompassing the transmembra ne domain adjacent to the isoform(s) of ?-? subunits of Na+-K+ ATPase. Considering the extraordinary importance of Na+-K+ ATPase in cellular function, several internationally established investigators have contributed their articles in the monograph entitled “Regulation of Membrane Na+-K+ ATPase” for inspiring young scientists and graduate students to enrich their knowledge on the enzyme, and we are sure that this book will soon be considered as a comprehensive scientific literature in the area of Na+-K+ ATPase regulation in health and disease.

P-type atpases

Название: P-type atpases
ISBN: 1493931784 ISBN-13(EAN): 9781493931781
Издательство: Springer
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Описание:

1. An Introduction to P-type ATPase research

Poul Nissen

Part I: Protein Production, Isolation, Purification, and Stabilization

2. Purification of Na, K-ATPase from Pig Kidney

Natalya U. Fedosova

3. Preparation of Ca2+-ATPase1a Enzyme from Rabbit Sarcoplasmic Reticulum

Jesper V. M ller and Claus Olesen

4. Isolation of H+/K+-ATPase-enriched Membrane Fraction from Pig Stomachs

Kazuhiro Abe and Claus Olesen

5. Overproduction of PiB-type ATPases

Xiangyu Liu, Oleg Sitsel, Kaituo Wang, and Pontus Gourdon

6. Coordinated Overexpression in Yeast of a P4-ATPase and its Associated Cdc50 Subunit: The Case of the Drs2p/Cdc50p Lipid Flippase Complex

Hassina Azouaoui, Cйdric Montigny, Aurore Jacquot, Raphaлlle Barry, Philippe Champeil, and Guillaume Lenoir

7. The Plasma Membrane Ca2+-ATPase: Purification by Calmodulin Affinity Chromatography, and Reconstitution of the Purified Protein

Verena Niggli and Ernesto Carafoli

8. Expression of Na, K-ATPase and H, K-ATPase Isoforms With The Baculovirus Expression System

Jan B. Koenderink and Herman G.P. Swarts

9. Time-dependent Protein Thermostability Assay

Ilse Vandecaetsbeek and Peter Vangheluwe

Part II: Activity Assays

10. Colorimetric Assays of Na, K-ATPase

Kathleen J. Sweadner

11. ATPase Activity Measurements by an Enzyme-Coupled Spectrophotometric Assay Pankaj Sehgal, Claus Olesen, and Jesper V. M ller

12. Antimony-Phosphomolybdate ATPase Assay

Gianluca Bartolommei and Francesco Tadini-Buoninsegni

13. ATPase Activity Measurements using radiolabeled ATP

Herman G.P. Swarts and Jan B. Koenderink

14. Assaying P-type ATPases Reconstituted in Liposomes

Hans-Jьrgen Apell and Bojana Damnjanovic

15. Coupling ratio for Ca2+ Transport by Calcium Oxalate Precipitation

Pankaj Sehgal, Claus Olesen, and Jesper V. M ller

16. Calcium Uptake in Crude Tissue Preparation

Philip A. Bidwell and Evangelia G. Kranias

17. Measuring H+ Pumping and Membrane Potential Formation in Sealed Membrane Vesicle Systems

Alex Green Wielandt, Michael G. Palmgren, Anja Thoe Fuglsang, Thomas Gьnther Pomorski, and Bo H jen Justesen

18. Assay of Flippase Activity in Proteoliposomes using Fluorescent Lipid Derivatives Magdalena Marek and Thomas Gьnther Pomorski

Part III: In vitro Functional Studies

19. The use of Metal Fluoride Compounds as Phosphate Analogs for Understanding the Structural Mechanism in P-type ATPases

Stefania J. Danko and Hiroshi Suzuki

20. Phosphorylation/Dephosphorylation Assays

Hiroshi Suzuki

21. Tryptophan Fluorescence Changes Related to Ca2+-ATPase Function

Pankaj Sehgal, Claus Olesen, and Jesper V. M ller

Part IV: Ligand Binding Studies

22. Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca2+-ATPase by Competitive Inhibition of [g-32P]TNP-8N3-ATP Photolabeling

Johannes D. Clausen, David B. McIntosh, David G. Woolley, and Jens Peter Andersen

23. Ca2+ Binding and Transport Studied with Ca2+/EGTA Buffers and 45Ca2+

Pankaj Sehgal, Claus Olesen, and Jesper V. M ller

24. Assay of Copper Transfer and Binding to P1B-ATPases

Teresita Padilla-Benavides and Josй M. Argьello


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