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2 edition of ATPase activity and Ca2 plus transport properties of rat liver plasma membranes. found in the catalog.

ATPase activity and Ca2 plus transport properties of rat liver plasma membranes.

Mark Anthony Birch-Machin

ATPase activity and Ca2 plus transport properties of rat liver plasma membranes.

by Mark Anthony Birch-Machin

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Published by University of East Anglia in Norwich .
Written in English


Edition Notes

Thesis (Ph.D.), University of East Anglia, School of Biological Sciences, 1987.

ID Numbers
Open LibraryOL13848488M

  The sarcoplasmic reticulum Ca2+-ATPase, a P-type ATPase, has a critical role in muscle function and metabolism. Here we present functional studies and three new crystal structures of the rabbit. T1 - Change in plasma membrane Ca2+-ATPase splice-variant expression in response to a rise in intracellular Ca2+ AU - Zacharias, David A. AU - Strehler, Emanuel E. PY - / Y1 - / N2 - Background: Most eukaryotic genes are divided into introns and by:

Hepatic (Na +, K +)‐ATPase: A current view of its structure, function and localization in rat liver as revealed by studies with monoclonal antibodies Hyam L. Leffert M. D. Corresponding Author. Departments of Medicine, Neurosciences and Biology, University of California, San Diego, La Jolla, California Cited by:   The NAD+ metabolite cADP-Rib (cADPR) elevates cytosolic free Ca2+ in plants and thereby plays a central role in signal transduction pathways evoked by the drought and stress hormone abscisic acid. cADPR is known to mobilize Ca2+ from the large vacuole of mature cells. To determine whether additional sites for cADPR-gated Ca2+ release reside in plant cells, microsomes from Cited by:

We have shown that ouabain activates Src, resulting in subsequent tyrosine phosphorylation of multiple effectors. Here, we tested if the Na + /K +-ATPase and Src can form a functional signaling LLC-PK1 cells the Na + /K +-ATPase and Src colocalized in the plasma scence resonance energy transfer analysis indicated that both proteins were in close proximity, suggesting. The plasma membrane Ca2+-ATPase (PMCA) is a ubiquitously expressed protein, which constitutes a high affinity system extruding Ca2+ outside the cell and maintains the intracellular Ca2+ in the submicromolar range in a resting by: 1.


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ATPase activity and Ca2 plus transport properties of rat liver plasma membranes by Mark Anthony Birch-Machin Download PDF EPUB FB2

Furthermore, attempts by Lin [11] to reconstitute the purified Ca2+-ATPase from rat liver plasma membranes into artificial liposomes have shown an absence of ATP-depen- dent Ca2+ transport activity.

If the Ca2÷-ATPase does not function ~s the liver plasma membrane Ca2+ pump, it may act as an ectoenzyme [37,38] which would regulate the Cited by: 8. Rat liver plasma membranes contained a high affinity Ca 2+-ATPase which had an apparent half saturation constant of μM for Ca 2+-ATPase was not stimulated by adding magnesium and/or sely, the addition of these substances diminished the calcium-stimulation of Cited by:   Calcium transport and phosphorylated intermediate of (Ca2+ + Mg2+)-ATPase in plasma membranes of rat liver.

Chan KM, Junger KD. We have identified and characterized calcium transport and the phosphorylated intermediate of the (Ca2+ + Mg2+)-ATPase in plasma membrane vesicles prepared from rat by: Properties of Na+, K+-ATPase of liver plasma membranes in the hamster. Poupon RE, Le Quernec L, Erlinger S.

This study was designed to establish the properties of liver plasma membranes (LPM) Na+,K+-ATPase in the hamster and to determine whether a similar assay may be used to measure enzyme activity in the hamster and in the : Renée E.

Poupon, Loetitia Le Quernec, Serge Erlinger. The plasma membrane Ca 2+ ATPase (PMCA) is a transport protein in the plasma membrane of cells and functions to remove calcium (Ca 2+) from the function is vital for regulating the amount of Ca 2+ within all eukaryotic cells.

There is a very large transmembrane electrochemical gradient of Ca 2+ driving the entry of the ion into cells, yet it is very important that they maintain low. The activating mechanism of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on (Ca2+−Mg2+)-ATPase in the plasma membranes of rat liver was investigated.

(Ca2+−Mg2+)-ATPase activity was markedly increased by a sulfhydryl (SH) group protecting reagent dithiothreitol (DTT; and 5 mM as a final concentration), while the enzyme activity was significantly decreased by a Cited by: Abstract.

The alteration of (Ca 2+-Mg 2+)-ATPase activity in the plasma membranes of regenerating rat liver after a partial hepatectomy was was surgically removed about two thirds of that of sham-operated rats. The reduced liver weight by partial hepatectomy was restored about 50% at 24 h after the surgery, and it was completely restored at 72 by: The Ca 2+-stimulated, Mg 2+-dependent ATPase from rat liver plasma membranes was solubilized using the detergent polyoxyethylene 9 lauryl ether and purified by column chromatography using Polybuffer Exchan concanavalin A-Sepharose 4B, and Sephadex GThe molecular weight of the enzyme, estimated by gel filtration in the presence of the detergent on a Sephadex G column, Cited by: PDF | The Ca2+-pumping ATPase of plasma membrane, known to exist since [13], has now been characterized as a high Ca2+ affinity enzyme, present in | Find, read and cite all the research.

Plasma membrane calcium-transporting ATPase 1 is a plasma membrane Ca 2+ ATPase, an enzyme that in humans is encoded by the ATP2B1 gene.

It's a transport protein, a translocase, a calcium pump EC The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction s: ATP2B1, ATPase, Ca++ transporting.

ATPase) activity. Membranes from myometria of rats treated with progesterone lacked both basal and oxy-tocin-inhibited (Ca 2+ + Mg2+)-ATPase activities.

The oxytocin-inhibited enzyme also was found in plasma membranes from rat adipocytes, which are oxytocin target cells, but not from a nontarget tissue like duo-denal smooth muscle.

In this work, we show that MB stimulates the Ca2+-ATPase activity of the plasma membrane Ca2+-ATPase (PMCA) in human tissues from AD-affected brain.

Abstract. Complementary DNAs for two isoforms of the plasma membrane Ca2+-ATPase from rat brain have been isolated. The cDNAs were identified using an oligonucleotide probe derived from a conserved amino acid sequence of the ATP binding site of the aspartylphosphate family of transport ATPases.

The plasma membrane Ca2+-ATPase is a pump that functions in the primary active transport of Ca2+ at the plasma membrane. What features do you expect of this pump and the cellular environment. Choose all that apply: It transports Na+ and K+ ions. It is an antiporter. ATP2B3 antibody, N-term - ATPase plasma membrane Ca2+ transporting 3, 50 μg supplied Price: $ + $ shipping.

The plasma membrane Ca2+-ATPase is a pump that functions in the primary active transport of Ca2+ out of the cell. What features do you expect of this pump and the cellular environment. Choose all that apply.

A)It transports Na+ and K+ ions B)It is an antiporter C)The extracellular Ca2+ concentration is higher than the intracellular Ca2. properties distinguish it from other basic isoforms. It possesses the highest resting activity and calmodulin sensitivity, and represents more than 30–40% of the total pump protein in mature neurons [21].

Thus, PMCA2 is thought to be the principal ATPase that maintains Ca2+ homeostasis following neural excitation. TheCited by: Plasma membrane calcium ATPase isoform 3 expression in single cells isolated from rat liver -ATPase activity has been detected [17].

Nevertheless, specific PMCA isoforms expressed and their relevance in the phenomenon of activation in different liver cells remains Cited by: 7.

This editorial refers to ‘Endothelial nitric oxide synthase activity is inhibited by the plasma membrane calcium ATPase in human endothelial cells’ by M. Holton et al., pp. –, this issue. Nitric oxide (NO) is now seen as an important player in both normal cellular and whole-body physiology and also in many diseases including numerous vascular diseases such as hypertension Cited by: 1.

The PMCA pump is a minor component of the total protein of the plasma membrane (less than % of it). Quantitatively, it is overshadowed by the more powerful NCX in excitable tissue like heart; however, even cells in which the NCX predominates, the PMCA pump is likely to be the fine tuner of cytosolic Ca 2+, as it can operate in a concentration range in which the low affinity NCX is.

Key Words: Ca2+-ATPase, thermal analysis, cholesterol, calcium Introduction The plasma membrane Ca 2+-ATPase [PM-(Ca)-ATPase] is a ubiquitous enzyme of eukaryotic cells [1]. This enzyme couples the hydrolysis of ATP to the transport of calcium from the cytoplasm .ATP2B1 ATPase plasma membrane Ca2+ transporting plasma membrane apical plasma membrane ATPase activity cell junction PDZ domain binding positive regulation of bone mineralization dendritic spine membrane neuronal cell body membrane ion transmembrane transport membrane raft metal ion binding regulation of cytosolic.The aim of this study was to determine whether changes in protein content and/or gene expression of Na +-K +-ATPase subunits underlie its decreased enzyme activity during ischemia and measured protein and mRNA subunit levels in isolated rat hearts subjected to 30 min of ischemia and 30 min of reperfusion (I/R).