Energy Transductions by an Electrochemical Gradient of Sodium Ions

1990 ◽  
pp. 114-127 ◽  
Author(s):  
P. Dimroth
Keyword(s):  
Sodium Ions ◽  
Electrochemical Gradient

MODIFICATION OF DIRECT POTENTIOMETRIC METHOD FOR DETERMINING SODIUM IONS IN TECHNOLOGICAL AND WASTE SOLUTIONS OF HYDROMETALLURGICAL PRODUCTION

Mendeleev ◽  
2019 ◽  
Vol 2 (2) ◽  
Author(s):  
Sergey Aronbaev ◽  
Sitora Zhuraeva ◽  
Aminjon Umarov ◽  
Alexander Kim ◽  
Dmitry Aronbaev
Keyword(s):  
Potentiometric Method ◽  
Sodium Ions

ИЗУЧЕНИЕ СТРУКТУРЫ ДНК В ПЛЕНКАХ МЕТОДОМ ИК-ФУРЬЕ-СПЕКТРОСКОПИИ

2020 ◽  
Vol 65 (6) ◽  
pp. 1058-1064
Author(s):  
С.В. Пастон ◽  
◽  
А.М. Поляничко ◽  
О.В. Шуленина ◽  
Д.Н. Осинникова ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Hydration Shell ◽  
Aqueous Environment ◽  
Ir Absorption ◽  
Sodium Ions ◽  
High Molecular Weight Dna ◽  
Dna Hydration ◽  
Na Ions ◽  
Phosphate Groups ◽  
Dna Film

The aqueous environment and ionic surrounding are the most important factors determining the conformation of DNA and its functioning in the cell. The specificity of the interaction between DNA and cations is especially pronounced with a decrease in water activity. In this work, we studied the B-A transition in high molecular weight DNA with a decrease of humidity in the film with different contents of Na+ ions using FTIR spectroscopy. The IR spectrum of DNA is not only very sensitive to the state of its secondary structure, but also allows us to estimate the amount of water bound to DNA. Upon dehydration of the DNA film, changes characteristic of the B-A transition were observed in the IR absorption spectrum. Using thermogravimetric analysis, it was shown that the degree of DNA hydration reaches the saturation level at a relative humidity of 60% and decreases slightly upon further drying. It has been established that with increasing Na+ concentration, the amount of water strongly bound to DNA decreases. Along with it, sodium ions destroy the hydration shell of DNA and are able to interact directly with phosphate groups.

Chromo-ionophoric Properties of para-(5-phthalhydrazide-azo)-phenylene-N-aza-15-crown-5 in the Presence of Lithium and Sodium Ions

2008 ◽  
Vol 59 (10) ◽  
Author(s):  
Rodica Daniela Baratoiu ◽  
Radu Socoteanu ◽  
Radu Cristian Mutihac ◽  
Anca Elena Barbu ◽  
Adrian Beteringhe ◽  
...  
Keyword(s):  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Reversed Phase ◽  
Complex Stability ◽  
Sodium Ions ◽  
Layer Chromatography

Investigations on the hydrophobic and ionophoric character of para-(5-phthalhydrazide-azo)-phenylene-N-aza-15-crown- (1) were carried out by reversed phase thin layer chromatography (RP-TLC) and spectrophotometric measurements. The study included complexes with Li+ and Na+ cations (as perchlorates in acetonitrile and as dibenzyldithiocarbamate salts in chloroform). In both cases, the stoichiometry of complexes was 1:1:1 (1:M+:anion pair). The complex stability (logKS ) is similar.

The role of sodium ions in the thermoluminescence peaks of laboratory-irradiated natural quartz

2021 ◽  
Vol 141 ◽  
pp. 106539
Author(s):  
Tran Ngoc ◽  
Ho Van Tuyen ◽  
Le Anh Thi ◽  
Le Xuan Hung ◽  
Nguyen Xuan Ca ◽  
...  
Keyword(s):  
Sodium Ions ◽  
Natural Quartz

scholarly journals Sodium ions as substitutes for protons in the gastric H,K-ATPase

1989 ◽  
Vol 264 (30) ◽  
pp. 17854-17859
Author(s):  
C Polvani ◽  
G Sachs ◽  
R Blostein
Keyword(s):  
Sodium Ions

scholarly journals Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Gianluca Trinco ◽  
Valentina Arkhipova ◽  
Alisa A. Garaeva ◽  
Cedric A. J. Hutter ◽  
Markus A. Seeger ◽  
...  
Keyword(s):  
Kinetic Mechanism ◽  
Protein Quantification ◽  
Detergent Solution ◽  
Sodium Ions ◽  
Binding Studies ◽  
Equilibrium Binding ◽  
Uptake Rates ◽  
Bona Fide ◽  
Inside Out

AbstractIt is well-established that the secondary active transporters GltTk and GltPh catalyze coupled uptake of aspartate and three sodium ions, but insight in the kinetic mechanism of transport is fragmentary. Here, we systematically measured aspartate uptake rates in proteoliposomes containing purified GltTk, and derived the rate equation for a mechanism in which two sodium ions bind before and another after aspartate. Re-analysis of existing data on GltPh using this equation allowed for determination of the turnover number (0.14 s−1), without the need for error-prone protein quantification. To overcome the complication that purified transporters may adopt right-side-out or inside-out membrane orientations upon reconstitution, thereby confounding the kinetic analysis, we employed a rapid method using synthetic nanobodies to inactivate one population. Oppositely oriented GltTk proteins showed the same transport kinetics, consistent with the use of an identical gating element on both sides of the membrane. Our work underlines the value of bona fide transport experiments to reveal mechanistic features of Na+-aspartate symport that cannot be observed in detergent solution. Combined with previous pre-equilibrium binding studies, a full kinetic mechanism of structurally characterized aspartate transporters of the SLC1A family is now emerging.

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