scholarly journals Potentiodynamics of the Zinc and Proton Storage in Disordered Sodium Vanadate for Aqueous Zn-Ion Batteries

2020 ◽  
Vol 12 (49) ◽  
pp. 54627-54636
Author(s):  
Xiaoqiang Shan ◽  
SaeWon Kim ◽  
A. M. Milinda Abeykoon ◽  
Gihan Kwon ◽  
Daniel Olds ◽  
...  
Keyword(s):  
Sodium Vanadate

Effects of Sodium Vanadate on Various Types of Vascular Smooth Muscles

1986 ◽  
Vol 23 (3) ◽  
pp. 113-124 ◽  
Author(s):  
Tomoko Shimada ◽  
Keiichi Shimamura ◽  
Satoru Sunano
Keyword(s):  
Smooth Muscles ◽  
Vascular Smooth Muscles ◽  
Sodium Vanadate

scholarly journals [Phosphotyrosine]protein phosphatase in rat brain. A major [phosphotyrosine]protein phosphatase is a 23 kDa protein distinct from acid phosphatase

1986 ◽  
Vol 239 (1) ◽  
pp. 155-162 ◽  
Author(s):  
M Okada ◽  
K Owada ◽  
H Nakagawa
Keyword(s):  
Acid Phosphatase ◽  
Molecular Mass ◽  
Rat Brain ◽  
Column Chromatography ◽  
Protein Phosphatase ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Sodium Vanadate ◽  
Nitrophenyl Phosphate ◽  
Phosphotyrosine Protein Phosphatase

A [phosphotyrosine]protein phosphatase (PTPPase) was purified almost to homogeneity from rat brain, with [32P]p130gag-fps, an oncogene product of Fujinami sarcoma virus, as substrate. The characteristics of the purified preparation of PTPPase were as follows: the enzyme was a monomer with a molecular mass of 23 kDa; its optimum pH was 5.0-5.5; its activity was not dependent on bivalent cations; its activity was strongly inhibited by sodium vanadate, but was not inhibited by ZnCl2, L(+)-tartrate or NaF; it catalysed the dephosphorylation of [32P]p130gag-fps, [[32P]Tyr]casein, p-nitrophenyl phosphate and L-phosphotyrosine, but did not hydrolyse [[32P]Ser]tubulin, L-phosphoserine, DL-phosphothreonine, 5′-AMP, 2′-AMP or beta-glycerophosphate significantly. During the purification, most of the PTPPase activity was recovered in distinct fractions from those of conventional low-molecular-mass acid phosphatase (APase), which was reported to be a major PTPPase [Chernoff & Li (1985) Arch. Biochem. Biophys. 240, 135-145], from DE-52 DEAE-cellulose column chromatography, and those two enzymes could be completely separated by Sephadex G-75 column chromatography. APase also showed PTPPase activity with [32P]p130gag-fps, but the specific activity was lower than that of PTPPase with molecular mass of 23 kDa, and it was not sensitive to sodium vanadate. These findings suggested that PTPPase (23 kDa) was the major and specific PTPPase in the cell.

Hydrogen reduced sodium vanadate nanowire arrays as electrode material of lithium-ion battery

2019 ◽  
Vol 26 (6) ◽  
pp. 1540-1549 ◽  
Author(s):  
Xue-liu Xu ◽  
Guang-zhong Li ◽  
Ze-wei Fu ◽  
Jun-tao Hu ◽  
Zhi-ping Luo ◽  
...  
Keyword(s):  
Lithium Ion Battery ◽  
Electrode Material ◽  
Lithium Ion ◽  
Nanowire Arrays ◽  
Sodium Vanadate

scholarly journals Sodium Vanadate Treatment as a Shortcut Following Alkaline Phosphatase Cleavage

BioTechniques ◽  
1998 ◽  
Vol 25 (3) ◽  
pp. 350-352 ◽  
Author(s):  
Yu-Yuan Peter Wo ◽  
Der-Shyan Sheu ◽  
Cheng-Hsiung Lu
Keyword(s):  
Alkaline Phosphatase ◽  
Sodium Vanadate

Cleaner production of vanadium oxides by cation-exchange membrane-assisted electrolysis of sodium vanadate solution

2017 ◽  
Vol 169 ◽  
pp. 440-446 ◽  
Author(s):  
Bo Pan ◽  
Wei Jin ◽  
Biao Liu ◽  
Shili Zheng ◽  
Shaona Wang ◽  
...  
Keyword(s):  
Cation Exchange ◽  
Vanadium Oxides ◽  
Cleaner Production ◽  
Cation Exchange Membrane ◽  
Sodium Vanadate ◽  
Exchange Membrane

Alkaloid Sequestration by Papaver somniferum Latex

1984 ◽  
Vol 39 (9-10) ◽  
pp. 876-881 ◽  
Author(s):  
B. C. Homeyer ◽  
Margaret F. Roberts
Keyword(s):  
Acid Medium ◽  
Considerable Increase ◽  
Papaver Somniferum ◽  
Sodium Vanadate ◽  
Medium Ph ◽  
Alkaloid Sequestration ◽  
Chlormadinone Acetate ◽  
Atpase Inhibitors

Abstract The 1000 x g organelles of Papaver somniferum latex have been shown to accumulate rapidly, large quantities of alkaloids (0.05- 1 mg/mg organelle protein), particularly morphine, thebaine, codeine and papaverine and have been found to exhibit a surprising degree of specificity for the accumulation of these alkaloids. The uptake of alkaloid is independent of temperature and does not show a requirement for ATP 10-3 ᴍ, Mg2+ 10-3 ᴍ, or KCl 10-3 ᴍ. It is unaffected by known ATPase inhibitors (chlormadinone acetate 2.5 × 10-5 ᴍ, N,N-dicyclohexylcarbo- diimide 5 × 10-4 ᴍ and sodium vanadate 10-4 ᴍ) but showed considerable increase in morphine accumulation in the presence of 4-chloromercumbenzoate 5 x 10-4 ᴍ, while N-methylmaleimide 5 × 10-4 ᴍ had no effect, and carbonylcyanide 4-(trifluoromethoxy)phenylhydrazone 5 × 10-4 ᴍ caused a reduction (ca. 30%) of morphine uptake. An acid medium, pH 4.5-5.5, also results in decreased morphine uptake.

scholarly journals Transport of a fluorescent macromolecule via endosomes to the vacuole in Saccharomyces cerevisiae.

1987 ◽  
Vol 104 (1) ◽  
pp. 67-75 ◽  
Author(s):  
M Makarow ◽  
L T Nevalainen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ammonium Chloride ◽  
Mammalian Cells ◽  
Extracellular Fluid ◽  
Endocytic Pathway ◽  
Sodium Vanadate ◽  
Energy Depletion ◽  
Internal Ph ◽  
Intermediate Compartment ◽  
Cytoplasmic Compartment

Fluorescein isothiocyanate-conjugated dextran (FITC-dextran) is internalized by endocytosis into the lysosome-like vacuoles of Saccharomyces cerevisiae (Makarow, M., 1985, EMBO (Eur. Mol. Biol. Organ.) J. 4:1861-1866). Here we show that under energy depletion conditions FITC-dextran accumulated in a cytoplasmic compartment, from which it could be chased to the vacuole when the energy block was removed. The internal pH of the intermediate compartment under energy depletion was determined by fluorometry to be 5.8. The pH could be raised by the lysosomotropic agent ammonium chloride, the protonophore carbonyl cyanide p-trifluoromethoxyphenyl-hydrazone (CCCP) and the ATPase inhibitors dicyclohexylcarbodiimide (DCCD) and sodium vanadate. The pH of the vacuole was found to be 6.5. It was raised by ammonium chloride, CCCP, and DCCD, but not with sodium vanadate. Efrapeptin had no effect on the internal pH of either compartment. By dissecting the endocytic pathway, two portions of the route leading to the vacuole could be studied separately. The internalization of FITC-dextran from the extracellular fluid to the intermediate compartment followed linear kinetics, was independent of energy, and occurred at temperatures of between 15 degrees and 37 degrees C. Transfer of the marker from the intermediate compartment to the vacuole required energy, took place at temperatures between 19 degrees and 37 degrees C, and had a half-time of 7 min at 37 degrees C. Transport of the marker from the exterior of the cell to the vacuole did not require acidic pH values in the intermediate compartment or the vacuole. We suggest that the cytoplasmic compartment revealed by FITC-dextran, under energy depletion, represents the equivalent of the endosomes of mammalian cells.

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