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Saturday, August 8, 2020 | History

3 edition of Ion-Motive Atpases found in the catalog.

Ion-Motive Atpases

Structure, Function, and Regulation (Annals of the New York Academy of Sciences)

  • 104 Want to read
  • 35 Currently reading

Published by New York Academy of Sciences .
Written in English

    Subjects:
  • Mathematics and Science,
  • Science/Mathematics,
  • Adenosine triphosphatase,
  • Biological transport, Active,
  • Congresses,
  • Ion channels

  • Edition Notes

    ContributionsErnesto Carafoli (Editor), Antonio Scarpa (Editor), Sergio Papa (Editor)
    The Physical Object
    FormatPaperback
    Number of Pages515
    ID Numbers
    Open LibraryOL8267276M
    ISBN 100897667700
    ISBN 109780897667708

    The P-type ATPases, also known as E 1-E 2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation (hence P) of a key conserved aspartate residue within the pump and their energy source, adenosine Missing: Ion-Motive. The mediators of these fundamental processes are ion-motive ATPases, highly conserved enzymes that play key roles in cell physiology from bacteria to man. As the first comprehensive overview of this important class of enzymes, this handbook summarizes recent knowledge about the molecular mechanism of ATPases, relating this information to the.

    The Na +,K +-ATPase is an ubiquitous plasma membrane protein complex that belongs to the P-type family of ion motive normal conditons, it couples the hydrolysis of one molecule of ATP to the exchange of three Na + for two K + ions, thus maintaining the normal gradient of these cations in animal cells. Despite decades of investigation of its structure and function, the structural. Book title: Acid-Base Balance and Nitrogen Excretion in Invertebrates – Mechanisms and Strategies in various Invertebrate Groups with Considerations of Challenges caused by Ocean Acidification. Ion-motive ATPases and active, transbranchial NaCl uptake in the red freshwater crab, Dilocarcinus pagei (Decapoda, Trichodactylidae). Journal of.

    After his postdoctoral research on the molecular and cell biological aspects of membrane proteins such as acetylcholine receptors and ion-motive ATPases at Cornell University and the Johns Hopkins University, he joined the University of Virginia as an assistant professor in and started to utilize atomic force microscopy (AFM) in biological : Hardcover. Structure. There are three important classes of ion motive ATPases (P-type, F 0-F 1, and vacuolar) that are different from one another both in terms of structure and the source of chemical energy required to sustain ion P-type ATPase is the most widely distributed and occurs in the surface membrane of nearly all animal cells.


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Ion-Motive Atpases Download PDF EPUB FB2

BiophysicalJournal vol. 59, a TU-Pos EFFECT OF MEMBRANE VOLTAGE ON THE PLASMA MEMBRANE H+-ATPASE OF SACCHAROMYCES CEREVISIAE. Donna Seto-Young and David S. Perlin. Dept.

of Biochemistry, The Public Health Research Institute, New York, N.Y, The effects of membrane voltage on the plasma. The reverse process, transforming an ion imbalance into chemical energy, drives mitochondrial and chloroplast ATP synthesis. The mediators of these fundamental processes are ion-motive ATPases, highly conserved enzymes that play key roles in cell physiology from bacteria to man.

Print book: Conference publication: EnglishView all editions and formats: Rating: (not yet rated) 0 with reviews - Be the first. Subjects: Adenosine triphosphatase -- Congresses. Ion channels -- Congresses. Biological transport, Active -- Congresses.

View all subjects; More like this: Similar Items. The mediators of these fundamental processes are ion-motive ATPases, highly conserved enzymes that play key roles in cell physiology from bacteria to man. This handbook summarizes recent knowledge about the molecular mechanism of ATPases, relating this information to the physiology and pathophysiology of Ion-Motive Atpases book transport, mitochondrial function.

The Na + /K +-ATPase, a membrane-associated ion-motive ATPase, uses energy from the hydrolysis of ATP to move Na + out of and K + into cells. We have labeled ATPase isolated from duck supraorbital salt glands with one of Cy3-maleimide, and Alexa Fluor carboxylic acid, succinimidyl ester.

One of ion-regulating enzymes is classified as ion motive adenosine triphosphatase (ATPase). Ion motive ATPases exchange two different ions across the membrane at the expense of ATP energy. ATPases involved in ion translocation are present in a diverse variety of biological membranes.

Three major classes of these ‘ion motive’ enzymes, designated here as ‘P’ (phosphorylated), ‘V’ (vacuolar), and ‘F’ (F 0 F 1), are now known to exist. In addition to the regulation of intracellular ionic or pH balance, some ATPases help drive numerous physiological or biological processes by ‘energy coupling’.Cited by:   Amyloid beta-peptide impairs ion-motive ATPase activities: evidence for a role in loss of neuronal Ca2+ homeostasis and cell death These data suggest that impairment of ion-motive ATPases may play a role in the pathogenesis of neuronal injury in Alzheimer's disease.

Articles from The Journal of Neuroscience are provided here courtesy of. A New Efficient Strategy to Reconstitute Membrane Proteins into Liposomes substrate carriers, energy-conserving enzymes involved in oxidative phosphorylation and ion motive ATPases (Racker, Levy D.

() A New Efficient Strategy to Reconstitute Membrane Proteins into Liposomes: Application to the Study of Ca. A proton-pump inhibitor expedition: the case histories of omeprazole and esomeprazole.

the case histories of omeprazole and esomeprazole. Ion motive ATPases: V- and P-types ATPases. Chapters 9 and 10 of this excellent book concern the energetics and mechanisms of transport, and Chapter 4 is a discussion of the energy of ion gradients.

Jain, M.K. () Introduction to Biological Membranes, 2nd edn, John Wiley & Sons, Inc., New York. A textbook of membranology, longer and more aduanced than Finean et al. New models of the gastric H,K ATPase in the E1K and E2P states are presented as the first structures of a K+ counter-transport P2-type ATPase exhibiting ion entry and exit paths.

Homology modeling was first used to generate a starting conformation from the srCa ATPase E2P form (PDB code 1wpg) that contains bound MgADP.

Energy minimization of the model showed a conserved adenosine site but Missing: Ion-Motive. These are two of a class of proteins called """""Ion-motive ATPases""""", enzymes that use the energy of ATP to pump ions across cell membranes. Ion pumps play an important role in all cells, and disordered function of these enzymes is associated with human disease, including heart failure.

The gastric hydrogen potassium ATPase or H + /K + ATPase is the proton pump of the stomach. It exchanges potassium from the intestinal lumen with cytoplasmic hydronium [2] and is the enzyme primarily responsible for the acidification of the stomach contents and the activation of the digestive enzyme pepsin [3] (see gastric acid).Missing: Ion-Motive.

ion-motive ATPases in the anterior and posterior gills of D. pagei. We also provide electrophysiological data that support a role for apical V-ATPases in active, transbranchial Cl– uptake.

Materials and methods Crabs Intermoult Dilocarcinus pagei Stimpson, measuring –cm carapace width, were collected from a temporary. The present investigation examined the microanatomy and mRNA expression and activity of ion-motive ATPases, in anterior and posterior gills of a South American, true freshwater crab, Dilocarcinus pagei.

Like diadromous crabs, the anterior gills of this hololimnetic trichodactylid exhibit a highly attenuated (2–5 μm), symmetrical epithelium on both lamellar surfaces.

from book The Plant Plasma Membrane Pedersen PL, Carafoli E () Ion motive ATPases. Trends Biochem Sci – Pedersen BP, Buch-Pedersen MJ, Morth JP, Palmgren MG, Nissen P ( COVID Resources.

Reliable information about the coronavirus (COVID) is available from the World Health Organization (current situation, international travel).Numerous and frequently-updated resource results are available from this ’s WebJunction has pulled together information and resources to assist library staff as they consider how to handle coronavirus.

classes of ion-motive ATPases: domain characterization and directed mutagenesis to identify sites ofbindingandoftransport. However, the book does include coverage of subunit membrane architecture, on whichworkhas progressed nicely. Thefact that the V-type pumps function in vivo as true ATPases, unlike the F-type pumps, perhaps deserves more.

Welcome,you are looking at books for reading, The mediators of these fundamental processes are ion-motive ATPases, highly conserved enzymes that play key roles in cell physiology from bacteria to man. As the first comprehensive overview of this important class of enzymes, this handbook summarizes recent knowledge about the molecular.

This ATPase activity is generally the easiest way of identifying them. Pumps are membrane-embedded enzymes that couple the hydrolysis of ATP to active translocation of ions across the membrane.

The central issue of ion motive ATPases is to couple the hydrolysis of ATP (and their auto-phosphorylation) to the translocation of ions. The Na/K-ATPase pump.P type ion motive ATPases of Helicobacter pylori; K.

Melchers, et al. 8. Which is the most important factor in duodenal ulcer pathogenesis: the strain of Helicobacter pylori or the host?

D.Y. Graham, et al. 9. The effect of Helicobacter pylori on the surface hydrophobicity and phospholipid composition of the gastric mucosa; L.M. Lichtenberger. Price: $There are P-type ATPases of different specificity with respect to the transported substrate(s). In animal cells, P-type ATPases are known for uniport, e.g., of Ca 2+ (review: Carafoli ) or H + (Kinne-Saffran ) and for antiport, e.g., of H + /K + (Forte et al.

) or of Na + /K + (Skou ), the latter being probably the most familiar Missing: Ion-Motive.