Low-temperature Raman spectroscopy of sodium-pump rhodopsin from Indibacter alkaliphilus: Insight of Na+ binding for active Na+ transport

2020 ◽  
Author(s):  
Yushi Nakamizo ◽  
Tomotsumi Fujisawa ◽  
Takashi Kikukawa ◽  
Akiko Okamura ◽  
Hiroaki Baba ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Structural Change ◽  
Low Temperature ◽  
Sodium Pump ◽  
Na Transport ◽  
Na Pump ◽  
Raman Measurement

We carried out the low-temperature Raman measurement of a sodium pump rhodopsin from Indibacter alkaliphilus (IaNaR) and examined the primary structural change for the light-driven Na+ pump. We observed that...

scholarly journals Autoradiographic localization of tritiated ouabain-sensitive sodium pump sites in ion transporting epithelia.

1980 ◽  
Vol 28 (1) ◽  
pp. 72-77 ◽  
Author(s):  
S A Ernst ◽  
J W Mills
Keyword(s):  
Sodium Pump ◽  
Close Correlation ◽  
Electrolyte Transport ◽  
Na Transport ◽  
Ouabain Binding ◽  
Intact Tissue ◽  
Na Pump ◽  
Saturation Kinetics ◽  
A Cell ◽  
Heterogeneous Tissues

The freeze-dry autoradiographic method devised originally by Stirling (J Cell Biol 53:704, 1972) to localize Na+ pump sites with (3H)ouabain is reviewed. Biochemical, physiological, and autoradiographic data are discussed which establish that ouabain binding to intact tissue conforms to rigid criteria for high Na+ pump specificity. Among these are that glycoside binding exhibits saturation kinetics, ligand dependence, and close correlation with degrees of inhibition of Na+-K+-ATPase and Na+ transport. Moreover, localization of Na+ pump sites by this technique shows a cell and membrane specificity which mirrors that obtained by cytochemical and immunocytochemical methods. In addition to resolving cell-specific patterns of localization in heterogeneous tissues, the demonstration of Na+-K+-ATPase by these techniques indicates that Na+ pumps are distributed uniformly along plasmalemmal surfaces and are restricted to the basolateral interface in reabsorptive and secretory epithelia despite the opposing polarity of net transepithelial electrolyte transport.

Raman spectroscopy study of acetonitrile at low temperature

2021 ◽  
Vol 246 ◽  
pp. 119065
Author(s):  
Shuo Zhang ◽  
Hongsheng Jia ◽  
Mingxing Song ◽  
He Shen ◽  
Li Dongfei ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Low Temperature ◽  
Spectroscopy Study

Effects of dietary Ca2+ on erythrocyte Na+-transport systems in spontaneously hypertensive rats

1991 ◽  
Vol 81 (1) ◽  
pp. 107-112 ◽  
Author(s):  
K. Fujito ◽  
M. Yokomatsu ◽  
N. Ishiguro ◽  
H. Numahata ◽  
Y. Tomino ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Spontaneously Hypertensive Rats ◽  
Transport Systems ◽  
Hypertensive Rats ◽  
Na Transport ◽  
Spontaneously Hypertensive ◽  
Na Pump ◽  
Wistar Kyoto ◽  
Increased Activity ◽  
Regulation Of Blood Pressure

1. The purpose of this study was to determine the effect of dietary Ca2+ intake on blood pressure and erythrocyte Na+ transport in spontaneously hypertensive rats. 2. Spontaneously hypertensive rats and Wistar-Kyoto rats were fed diets with three different Ca2+ contents, 0.1% (low-Ca2+ diet), 0.6% (normal-Ca2+ diet) and 4.0% (high-Ca2+ diet), between 6 and 20 weeks of age. At 20 weeks of age, the levels of erythrocyte Na+ efflux, as well as Na+ and K+ contents in erythrocytes, were measured. 3. On the low-Ca2+ diet, spontaneously hypertensive rats showed an enhancement of hypertension. Conversely, on the high-Ca2+ diet, they showed an attenuation of the increase in blood pressure. Spontaneously hypertensive rats had a lower erythrocyte Na+ content and increased activity of the Na+ pump at higher levels of dietary Ca2+. Passive Na+ permeability and Na+-K+ co-transport were similar in spontaneously hypertensive rats on the low-, normal- and high-Ca2+ diets. There were no significant differences in blood pressure and in Na+ pump activity in WKY on the three different diets. 4. It is concluded that dietary Ca2+ might affect the regulation of blood pressure in spontaneously hypertensive rats by changing the activity of Na+ pump in the cell membrane.

Shining light on low-temperature methanol aqueous-phase reforming using homogeneous Ru-pincer complexes – operando Raman-GC studies

2017 ◽  
Vol 2 (3) ◽  
pp. 390-396 ◽  
Author(s):  
Vinzent Strobel ◽  
Julian Jonathan Schuster ◽  
Andreas Siegfried Braeuer ◽  
Lydia Katharina Vogt ◽  
Henrik Junge ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Low Temperature ◽  
Aqueous Phase ◽  
Volume Flow ◽  
Pincer Complexes ◽  
Methanol Reforming ◽  
Aqueous Phase Reforming ◽  
Flow Monitoring ◽  
Insight Into

A combination of operando Raman spectroscopy with online GC and volume-flow monitoring allows rapid insight into low-temperature methanol reforming.

Characteristics of active Na transport in intact cardiac cells

1979 ◽  
Vol 236 (2) ◽  
pp. H189-H199 ◽  
Author(s):  
H. G. Glitsch
Keyword(s):  
Heart Muscle ◽  
Muscle Cells ◽  
Cardiac Cells ◽  
Na Transport ◽  
Concentration Gradients ◽  
Experimental Conditions ◽  
Na Pump ◽  
Na Efflux ◽  
Heart Muscle Cells ◽  
K Concentration

An active Na transport maintains the Na and K concentration gradients across the cell membrane of many cells and restores them following excitation. Heart muscle cells display frequent electrical discharges and thus the cardiac Na pump is of fundamental functional significance. Some methods for studying active Na transport are described. The active Na efflux from heart muscle cells is activated by an increase in the intracellular Na and the extracellular K concentration. The linkage between active Na efflux and active K influx varies widely according to the experimental conditions. The cardiac Na pump is electrogenic and can contribute directly to the membrane potential of the cells. The effects of active Na transport on contraction and intercellular coupling in myocardium are discussed.

scholarly journals Effects of Dinitrophenol and Oligomycin on the Coupling between Anaerobic Metabolism and Anaerobic Sodium Transport by the Isolated Turtle Bladder

1966 ◽  
Vol 49 (3) ◽  
pp. 483-499 ◽  
Author(s):  
Neal S. Bricker ◽  
Saulo Klahr
Keyword(s):  
Sodium Transport ◽  
Anaerobic Metabolism ◽  
Sodium Pump ◽  
High Energy ◽  
Mitochondrial Atpase ◽  
Anaerobic Glycolysis ◽  
Anaerobic Conditions ◽  
Na Transport ◽  
Anaerobic System ◽  
Mitochondrial Atpase Activity

Dinitrophenol (1 x 10-5 M) has been found to inhibit anaerobic sodium transport by the isolated urinary bladder of the fresh water turtle. Concurrently, anaerobic glycolysis was stimulated markedly. However, tissue ATP levels diminished only modestly, remaining at approximately 75% of values observed under anaerobic conditions without DNP. The utilization of glucose (from endogenous glycogen) corresponded closely to that predicted from the molar quantities of lactate formed. Thus the glycolytic pathway was completed in the presence of DNP and if ATP were synthesized normally during glycolysis, synthesis should have been increased. On the other hand, the decrease in Na transport should have decreased ATP utilization. Oligomycin did not block sodium transport either aerobically or anaerobically, but ATP concentrations did decrease. When anaerobic glycolysis was blocked by iodoacetate, pyruvate did not sustain sodium transport thus suggesting that no electron acceptors were available in the system. Two explanations are entertained for the anaerobic effect of DNP: (a) Stimulation by DNP of plasma membrane as well as mitochondrial ATPase activity; (b) inhibition of a high energy intermediate derived from glycolytic ATP or from glycolysis per se. The arguments relevant to each possibility are presented in the text. Although definitive resolution is not possible, we believe that the data favor the hypothesis that there was a high energy intermediate in the anaerobic system and that this intermediate, rather than ATP, served as the immediate source of energy for the sodium pump.

A Low-Temperature Cell for Laser Raman Spectroscopy on Condensed Films and Nonvolatile Solids

1971 ◽  
pp. 276-279
Author(s):  
D. F. Shriver ◽  
B. Swanson ◽  
N. Nelson
Keyword(s):  
Raman Spectroscopy ◽  
Low Temperature ◽  
Laser Raman Spectroscopy ◽  
Laser Raman

A 19F nuclear magnetic resonance and Raman spectroscopic investigation of the reaction of iodine oxide pentafluoride with the Lewis acids, antimony and arsenic pentafluoride

1978 ◽  
Vol 56 (17) ◽  
pp. 2253-2258 ◽  
Author(s):  
Morley Brownstein ◽  
Ronald J Gillespie ◽  
John P. Krasznai
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Raman Spectroscopy ◽  
Magnetic Resonance ◽  
Low Temperature ◽  
Oxygen Atom ◽  
Spectroscopic Investigation ◽  
Lewis Acids ◽  
Raman Spectroscopic ◽  
Nuclear Magnetic

The reactions of IOF5 with SbF5 and with AsF5 have been investigated at low temperature by 19F nmr and Raman spectroscopy. It was found that SbF5 forms labile 1:1 and 2:1 complexes whereas AsF5 forms only a 1:1 complex. The IOF5 is bound through its oxygen atom to the Lewis acids AsF5, SbF5, or (SbF5)2.

Subcellular distribution of sodium pump isoform subunits in mammalian cardiac myocytes

1996 ◽  
Vol 270 (4) ◽  
pp. C1221-C1227 ◽  
Author(s):  
A. A. McDonough ◽  
Y. Zhang ◽  
V. Shin ◽  
J. S. Frank
Keyword(s):  
Guinea Pig ◽  
Driving Force ◽  
Human Heart ◽  
Sodium Pump ◽  
Immunogold Labeling ◽  
Guinea Pig Heart ◽  
Rat Cardiomyocytes ◽  
Adult Rat ◽  
Na Pump ◽  
T Tubules

The cardiac Na+ pump (Na+ -K+ -ATPase) provides the driving force for the Na+/Ca2+ exchanger, a determinant of intracellular Ca2+ stores. Three Na+ pump alpha-catalytic subunit isoforms are expressed in human heart, alpha1 and alpha2 are expressed in rat heart, and only alpha1 is expressed in guinea pig heart. The objective of this study was to determine whether there are isoform-specific patterns of expression in the transverse tubules (T tubules) vs. the peripheral sarcolemma. In adult rat cardiomyocytes, anti-alpha1-specific antibodies labeled the T tubules more intensely than the peripheral sarcolemma, in which labeling was patchy, the same pattern reported for distribution of the Na+/Ca2+ exchanger (J. S. Frank, G. Mottino, D. Reid, R. S. Molday, and K. D. Philipson, J. Cell Biol. 117: 337-345, 1992), whereas anti-alpha2- and anti-beta1-antibodies uniformly labeled T tubules and peripheral sarcolemma. In guinea pig cardiomyocytes, an anti-alpha-antibody against an extracellular epitope evenly labeled the peripheral sarcolemma and T tubules, and immunogold labeling demonstrated coincidence of alpha-subunits and intramembranous particles in sarcolemma. In summary, Na+ pumps are located in both peripheral sarcolemma and T tubules of cardiomyocytes expressing either multiple or single Na+ pump isoforms.

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