3 edition of Na/K-ATPase and related ATPases found in the catalog.
Na/K-ATPase and related ATPases
International Conference on the Na/K-ATPase and Related ATPases (9th 1999 Sapporo, Japan).
Includes bibliographical references.
|Other titles||Sodium/potassium-ATPase and related adenosine triphosphatases|
|Statement||editors Kazuya Taniguchi, Shunji Kaya.|
|Series||International congress series -- no. 1207|
|Contributions||Kaya, Shunji, Taniguchi, Kazuya, 1966-|
|LC Classifications||QP609.S63 I68 1999|
|The Physical Object|
|Pagination||xvii, 771 p. :|
|Number of Pages||771|
Exploring the Mechanism of Lipid Transport by a Flippase ATP-dependent flippases art closely related in their structures to ion pumps like the plasma membrane Na +, K +-ATPase and sarcoplasmic reticulum Ca 2+-ATPase, but they contend with a novel dilemma not shared by the ion transport systems. Consult the following reference and. summarize the. Purification of Na,K-ATPase expressed in Pichia Pastoris We have expressed the porcine α1/His10β1 subunits in Pichia pastoris (Strugatsky et al., ), a methanotrophic yeast which grows to high cell densities and provides a ready source of recombinant Na+/K+-ATPase.A recent.
P-type ATPases are a large group of evolutionary related ion and lipid pumps that have in common that they catalyze a transient phosphorylated intermediate at a key conserved aspartate residue within the pump in order to function. While all the P-type ATPases perform active transport across cellular membranes, they have different transport specificities and serve diverse physiological functions. Na+,K+-ATPase is an ATP-powered ion pump that establishes concentration gradients for Na+ and K+ ions across the plasma membrane in all animal cells by pumping Na+ from the cytoplasm and K+ from the extracellular medium. This heterodimeric enzyme, a member of P-type ATPases, is composed of a catalytic α-subunit with ten transmembrane domains and a heavily glycosylated auxiliary by: 1.
The Na + /K + ATPase pump is a pump found in the membrane of animal cell which uses the hydrolysis of ATP to pump 3Na + out of the cell and 2K + into the is a primary active transport and belongs to the family of P-type regulates the osmolarity of the cytosol by controlling the solute concentration inside the main function of the N+/K+ ATPase pump is to maintain. The Na+/K+ ATPase. a) Explain the role of the Na+/K+ ATPase in animal cells. b) This protein belongs to the P-type ATPase family. Explain briefly how P-type ATPases are different from other membrane ATPases (V-type, F-type, and ABC transporters). c) The Na+/K+ ATPase moves Na+ out of the cell.
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It includes a proposal that Na/K-ATPase plays a role as a tranducer of signal transduction, and, amongst other topics, covers the oligomericity of the enzyme, the site directed mutagenesis of P-type ATPases and the role of g-subunit.
The book will serve as an important resouce, not only for work on Na/K-ATPase, but also for the investigation of. Buy The Na/K- Atpase and Related Transport Atpases: Structure, Mechanism, and Regulation (Annals of the New York Academy of Sciences) on FREE SHIPPING on qualified orders.
P-type ATPases: These all form phosphorylated intermediates in the pump mechanism, like that shown for the Na,K-ATPase in Figure Among these are gastric H +-ATPase that is responsible for acidification of the stomach contents; Na +,K +-ATPase that is responsible for maintaining ionic gradients in most cells; PMCA (for plasma membrane calcium ATPase) responsible for pumping Ca 2+ out of.
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Transmembrane ATPases import many of the metabolites necessary for cell metabolism and export toxins, wastes, and solutes that can hinder cellular processes.
An important example is the sodium-potassium exchanger (or Na + /K + ATPase) that maintains the cell membrane another example is the hydrogen potassium ATPase (H + /K + ATPase or gastric proton pump) that acidifies BRENDA: BRENDA entry.
The Na/K pump, or Na,K-ATPase, is a key enzyme to the homeostasis of osmotic pressure, cell volume, and the maintenance of electrochemical gradients. Get this from a library. Na/K-ATPase and related ATPases: proceedings of the 9th International Conference on the Na/K-ATPase and related ATPases, Sapporo, Japan, August [Kazuya Taniguchi; Shunji Kaya;].
BRAIN Na +, K +-ATPase STRUCTURE. Na +, K +-ATPase is an olygomeric enzyme consisting of α and β subunits, both required for enzyme function (Fig.
(Fig.1). 1).Alpha subunit is the catalytic one which exists in different isoforms: α1, α2, α3, or α4, the latter identified only in testis ().The binding sites for ATP and the inhibitor ouabain as well as ion occlusion occur in α subunit ().Cited by: Na,K-ATPase and H,K-ATPases.
However, for Na,K-ATPase and H,K-ATPase, which consist of both ﬁ- andﬂ-subunits, there may be some detailed differences in regions of subunit interactions. Mutagenesis, proteolytic cleavage, and transition metal-catalyzed oxidative cleavages are providing much evidence about residues involved in bindingFile Size: 1MB.
ATPase is an enzyme. ATPase breaks down ATP into ADP and free phosphate ion, releasing energy. Just like lipase breaks down lipid. And lactase breaks down lactose, the same way ATPase breaks down ATP. ATP is the energy currency of the body. But w. 1 Na,K-ATPaseandRelatedP-typeTransportATPases:Structure, Biology,andMedicine.
GeoffreyHunt 2 GolgiCalciumPumpSecretoryPathwayCalciumATPase1 (SPCA1. Either you don't have an active Na,K-ATPase present or its activity is so low that it is superposed by other ATPases in the membrane or by a high phosphate background.
Cite 1 Recommendation. Lyophilized Na + /K +-ATPase was dissolved in water to a concentration of 1 U/ml, stored at °C in single-use aliquots and diluted with H 2 O to U/ml for use in the in vitro assay (final concentration in the assay U/ml). The data on inhibition of porcine Na + /K +-ATPase are presented in Supplementary Figure S7 and Supplementary Cited by: 6.
A Quick Assay for Na+-K+-ATPase Specific Activity DepartmentofBiology,RutgersUniversity, PennStreet,Camden,N.J,USA. Fax Cited by: Hebert H, Xian R, Thomsen K, Maunsbach AB () Structure of renal Na,K-ATPase as observed by cryo-EM of 2-D crystals.
In: Taniguchi K, Kaya S (eds) Na/K-ATPase and related ATPases. Elsevier, Amsterdam, pp 43–48 Google ScholarCited by: NA/K-ATPASE AND RELATED TRANSPORT ATPASES: Editors: LA Beauge, DC Gadsby, PJ Garrahan: Place of Publication: NEW YORK: Publisher: New York Academy of Sciences: Pages: Number of pages: 3: ISBN (Print) Publication status: Published - Event: VIIIth International Conference on the Na/K-ATPase (and Related Transport Cited by: 3.
I'd like to detect Na-K ATPase activity. Can the product Colorimetric ATPase Assay Kit () detect specific Na-K ATPase activity. This kit is intended for the measurement of ATPase activity, but is not specific to one particular type of activity. I would like to work with ecto-ntpdase enzymes in 4/5(1).
Due to the marked high expression of the Na + /K +-ATPase α3 subunit in T98G cells compared to LN and astrocytes, we tested a possible relationship between Na + /K +-ATPase and TMZ sensitivity.
To knockdown the Na + /K + -ATPase α3 subunit in T98G cells, cells were treated with stealth RNAi for 48 hrs to reduce the α3 subunit (Figure 7 A).Cited by: ATP1A3 A gene on chromosome 19q that encodes an enzyme belonging to the family of P-type cation transport ATPases and the subfamily of Na+/K+ -ATPases, the latter of which are responsible for establishing and maintaining electrochemical gradients of Na and K ions across the plasma membrane; they are required for osmoregulation in sodium-coupled transport of various organic and inorganic.
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 α- and β- subunits. At present four different α- (α-1,α-2,α-3 and α-4) and three β- (β-1, β-2, and β-3) isoforms have been identified in mammalian cells and their differential expressions Brand: Springer International Publishing.
This effect seems not to be related to the overall level of Na + /K +-ATPase resistance as indicated by the pronounced selectivity of gitoxigenin between lamb and non-adapted insect Na + /K +-ATPase and the relatively low discrimination of this compound between non-adapted insect and D.
plexippus-Na + /K + by: 6. The Na+/K+-ATPase generates ion gradients across the plasma membrane, essential for multiple cellular functions. In mammals, four different Na+/K+-ATPase α-subunit isoforms are associated with characteristic cell-type expression profiles and kinetics.
We found the zebrafish α2Na+/K+-ATPase associated with striated muscles and that knockdown causes a significant depolarization of the resting Cited by: P-type ATPases are a family of cation transport enzymes present in eukaryotes,archea and alpha helical bundle primary transportser (P-type ATPases) are known for catalysis of self phosphorylation of a key conserved aspartate residue within an ion pump.