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Vanadate

About: Vanadate is a research topic. Over the lifetime, 4497 publications have been published within this topic receiving 120109 citations. The topic is also known as: vanadate.


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Journal ArticleDOI
TL;DR: A comparison of the properties of the high affinity (Ca2+-Mg2+)-ATPase with those of the liver plasma membrane ATP-dependent Ca2+ transport activity reconstituted into artificial liposomes suggests that this high affinity

86 citations

Journal ArticleDOI
TL;DR: In this article, the effect of different chemical approaches on the size, morphology and size distribution of copper vanadate nanostructures in presence of Schiff-base ligand (N,N′-buthylenebis(acetylacetone iminato)dianion) was investigated.
Abstract: The effect of different chemical approaches on the size, morphology and size distribution of copper vanadate nanostructures in presence of Schiff-base ligand (N,N′-buthylenebis(acetylacetone iminato)dianion = acacbn) was investigated. The as-prepared products were characterized using X-ray diffraction, scanning electron microscopy, Fourier transform infrared spectrum, electron dispersive X-ray spectroscopy and ultraviolet–visible spectroscopy. The optical properties and photocatalytic activity of copper vanadate nano and bulk structures were compared by degradation of cationic dye methylene blue in aqueous solution under UV-light irradiation.

86 citations

Journal ArticleDOI
TL;DR: Luminescence and its decay lifetime studies confirm the decrease in non-radiative transition probability with the increase of heat treatment temperature and a possible reaction mechanism at different pH values is suggested in this study.
Abstract: GdVO4 : Ln3+ (Ln3+ = Dy3+, Eu3+, Sm3+, Tm3+) nanoparticles are prepared by a simple chemical route at 140 °C. The crystallite size can be tuned by varying the pH of the reaction medium. Interestingly, the crystallite size is found to increase significantly when pH increases from 6 to 12. This is related to slower nucleation of the GdVO4 formation with increase of VO43− present in solution. The luminescence study shows an efficient energy transfer from vanadate absorption of GdVO4 to Ln3+ and thereby enhanced emissions are obtained. A possible reaction mechanism at different pH values is suggested in this study. As-prepared samples are well dispersed in ethanol, methanol and water, and can be incorporated into polymer films. Luminescence and its decay lifetime studies confirm the decrease in non-radiative transition probability with the increase of heat treatment temperature. Re-dispersed particles will be useful in potential applications of life science and the film will be useful in display devices.

85 citations

Journal ArticleDOI
TL;DR: Three phenotypically distinct classes of mutant that have resulted from work on the yeast PMA1 H(+)-ATPase are reviewed, serving to identify critical parts of the polypeptide that are required for protein folding, conformational change and H( +):ATP coupling.
Abstract: One of the most abundant proteins in the yeast plasma membrane is the P-type H(+)-ATPase that pumps protons out of the cell, supplying the driving force for a wide array of H(+)-dependent cotransporters. The ATPase is a 100 kDa polypeptide, anchored in the lipid bilayer by 10 transmembrane alpha-helices. It is structurally and functionally related to the P-type Na(+),K(+)-, H(+),K(+)- and Ca(2+)-ATPases of animal cells and the H(+)-ATPases of plant cells, and it shares with them a characteristic reaction mechanism in which ATP is split to ADP and inorganic phosphate (P(i)) via a covalent beta-aspartyl phosphate intermediate. Cryoelectron microscopic images of the H(+)-ATPase of Neurospora crassa and the sarcoplasmic reticulum Ca(2+)-ATPase of animal cells have recently been obtained at 8 nm resolution. The membrane-embedded portion of the molecule, which presumably houses the cation translocation pathway, is seen to be connected via a narrow stalk to a large, multidomained cytoplasmic portion, known to contain the ATP-binding and phosphorylation sites. In parallel with the structural studies, efforts are being made to dissect structure/function relationships in several P-type ATPases by means of site-directed mutagenesis. This paper reviews three phenotypically distinct classes of mutant that have resulted from work on the yeast PMA1 H(+)-ATPase: (1) mutant ATPases that are poorly folded and retained in the endoplasmic reticulum; (2) mutants in which the conformational equilibrium has been shifted from the E(2) state, characterized by high affinity for vanadate, to the E(1) state, characterized by high affinity for ATP; and (3) mutants with altered coupling between ATP hydrolysis and proton pumping. Although much remains to be learned before the transport mechanism can be fully understood, these mutants serve to identify critical parts of the polypeptide that are required for protein folding, conformational change and H(+):ATP coupling.

85 citations

Journal ArticleDOI
TL;DR: It is concluded that the Golgi of corn coleoptiles contains a KCl-stimulated H(+)-ATPase which can acidify the interior of Golgi cisternae and associated vesicles.
Abstract: Corn (Zea mays L. cv Trojan T929) coleoptile membranes were fractionated on sucrose density gradients, and ATP-dependent proton pumping activity was localized by the techniques of [(14)C]methylamine uptake and quinacrine fluorescence quenching. Two peaks of proton pumping activity were detected: a light peak (1.07 grams/cubic centimeter) corresponding to the previously characterized tonoplast-type H(+)-ATPase, and a second peak (1.13 grams/cubic centimeter) which coincided with the Golgi markers, latent UDPase, and glucan synthase I. The second peak was lighter than that of the plasma membrane marker, uridine diphosphoglucose-sterol glucosyltransferase (1.16 grams/cubic centimeter) and was not inhibited by vanadate, an inhibitor of the plasma membrane ATPase. The activity was also better correlated with the Golgi cisternae marker, glucan synthase I, than with latent UDPase, a secretory vesicle marker, but a secretory vesicle location cannot be ruled out. The tonoplast-type and Golgi proton pumps were similar in several respects, including a pH optimum at 7.2, stimulation by chloride, inhibition by diethylstilbestrol and N,N'-dicyclohexylcarbodiimide (DCCD), insensitivity to oligomycin and azide, and nucleotide specificity for Mg(2+)-ATP. However, the Golgi H(+) pump was much less sensitive to nitrate and iodide, and more sensitive to the anion channel blockers, 4-acetamido-4'-isothiocyano-2,2'-stilbene sulfonic acid (SITS) and 4,4'-diisothiocyano-2,2'-stilbene disulfonic acid (DIDS) than the tonoplast-type H(+)-pump. The Golgi pump, but not the tonoplast-type pump, was stimulated by valinomycin in the presence of KCl. It is concluded that the Golgi of corn coleoptiles contains a KCl-stimulated H(+)-ATPase which can acidify the interior of Golgi cisternae and associated vesicles.

84 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023109
2022211
202178
202075
201996
201899