• The Korean Journal of Physiology
• /
• 제28권2호
• /
• pp.159-167
• /
• 1994

The contraction of rabbit basilar artery was examined as a function of changes in the $Na^+$ electrochemical gradient in order to determine the contribution of $Na^+/Ca^{2+}$ exchange to the modulation of contractility. Ouabain $(10^{-5}\;M)$ or $K^+-free$ Tyrode solution caused an increase in tonic tension even in the presence of a $Ca^{2+}$ channel blocker $(10^{-6}\;M\;verapamil)$ and an ${\alpha}-receptor$ blocker $(10^{-5}\;M\;phentolamine)$. After treatment with ouabain $(10^{-5}\;M)$, contractions were augmented by reduction of external $Na^+$ concentration. The longer the treatment with ouabain $(10^{-5}\;M)$ was, the larger the amplitude of $Na^+-free$ contracture was. $Na^+-free$ contracture wag induced by either substitution of equimolar Tris for $Na^+$ or substitution of equimolar $Li^+\;for\;Na^+$. The competition between $Na^+\;and\;Ca^{2+}$ for the $Na^+/Ca^{2+}$ exchange carrier would exist, because it was observed that contractility was dependent on the $Na^+$ electrochemical gradient or the extracellular $Ca^{2+}$ concentration (2 mM, 4 mM). Ryanodine $(10^{-7}\;M)$, the blocker of intracellular $Ca^{2+}$ release from the sarcoplasmic reticulum, did not suppress the development of $Na^+-free$ contracture. The contractile response to norepinephrine $(10^{-6}\;M)$ was augmented by reducing the extracellular $Na^+$ concentration. The relaxation rate from caffeine-induced contraction was dependent on the extracellular $Na^+$ concentration (0 mM, 140 mM). From the above results, it could be suggested that $Na^+/Ca^{2+}$ exchange can move $Ca^{2+}$ either into or out of rabbit basilar arterial smooth muscle. $Ca^{2+}$ entry or extrusion is dependent upon the $Na^+$ electrochemical gradient. $Na^+/Ca^{2+}$ exchange plays a significant role in the regulation of contractility in rabbit basilar arterial smooth muscle.

• 한국생물물리학회:학술대회논문집
• /
• 한국생물물리학회 2001년도 학술 발표회 진행표 및 논문초록
• /
• pp.45-45
• /
• 2001

The Na$^{＋}$-K$^{＋}$ pump, a plasma membrane Na$^{＋}$-K$^{＋}$ ATPase is plays a key role in the regulation and maintenance of Na$^{＋}$ and $K^{＋}$ ion concentration gradients across cell membranes. This enzyme pumps three Na$^{＋}$ out of and two $K^{＋}$ into the cell against their electrochemical gradient by utilizing the energy derived from ATP. Therefore, the Na$^{+}$-K$^{+}$ pump generates a net outward electrical current.(omitted)ted)

• Journal of Electrochemical Science and Technology
• /
• 제10권3호
• /
• pp.302-312
• /
• 2019

The voltage produced from the salinity gradient in reverse electrodialysis (RED) increases proportionally with the number of cell pairs of alternating cation and anion exchange membranes. Large-scale RED systems consisting of hundreds of cell pairs exhibit high voltage of more than 10 V, which is sufficient to utilize water electrolysis as the electrode reaction even though there is no specific strategy for minimizing the overpotential of water electrolysis. Moreover, hydrogen gas can be simultaneously obtained as surplus energy from the electrochemical reduction of water at the cathode if the RED system is equipped with proper venting and collecting facilities. Therefore, RED-driven water electrolysis system can be a promising solution not only for sustainable electric power but also for eco-friendly hydrogen production with high purity without $CO_2$ emission. The RED system in this study includes a high membrane voltage from more than 50 cells, neutral-pH water as the electrolyte, and an artificial NaCl solution as the feed water, which are more universal, economical, and eco-friendly conditions than previous studies on RED with hydrogen production. We measure the amount of hydrogen produced at maximum power of the RED system using a batch-type electrode chamber with a gas bag and evaluate the interrelation between the electric power and hydrogen energy with varied cell pairs. A hydrogen production rate of $1.1{\times}10^{-4}mol\;cm^{-2}h^{-1}$ is obtained, which is larger than previously reported values for RED system with simultaneous hydrogen production.

• Journal of Microbiology and Biotechnology
• /
• 제6권6호
• /
• pp.391-396
• /
• 1996

The Gram-negative marine bacterium Marinomonas vaga, which requires 0.5 M NaCl concentration for optimal growth, is slightly halophilic. The growth of M vaga was highly resistant to the proton conductor, carbonyl cyanide m-chlorophenylhydrazone (CCCP) under alkaline pH conditions (pH 8.5) but very sensitive to CCCP under acidic pH conditions (pH 6.5). These results suggest that the respiratory chain-linked NADH oxidase system of M. vaga may lead to generation of a $Na^{+}$ electrochemical gradient. In order to examine the existence of $Na^{+}$-stimulated NADH oxidase in M. vaga, membrane fractions were prepared by the osmotic lysis method. The membrane-bound NADH oxidase oxidized both NADH and deamino-NADH as substrates and required $Na^{+}$ for maximum activity. The maximum activity of NADH oxidase was obtained at about pH 8.5 in the presence of 0.2 M NaCl. The site of $Na^{+}$-dependent activation in the NADH oxidase system was at the NADH:quinone oxidoreductase segment. The NADH oxidase and NADH:quinone oxidoreductase were very sensitive to the respiratory chain inhibitor, 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO) in the presence of 0.2 M NaCl but highly resistant to another respiratory inhibitor, rotenone. Based on these findings, we conclude that M. vaga possesses the $Na^{+}$-dependent NADH:quinone oxidoreductase that may function as an electrogenic $Na^{+}$ pump.

• 멤브레인
• /
• 제27권2호
• /
• pp.109-120
• /
• 2017

양이온($Na^+$) 및 음이온($Cl^-$)이 각각의 CEM과 AEM을 통해 선택적으로 분리되어 담수로 이동할 때 발생되는 전위차와 산화/환원(redox couple)형 전해질을 포함하고 있는 전극에서 발생하는 전류를 이용하여 전기 에너지로 전환시키는 에너지변환장치이다. RED 시스템의 핵심소재 중 하나인 이온교환막은 높은 출력 밀도를 달성하기 위해 1) 낮은 팽윤거동, 2) 적절한 이온교환능, 3) 높은 이온전도도, 4) 높은 이온선택성을 만족시켜야 한다. 본 논문에서는 이를 만족시키는 소재 및 이온교환막의 연구동향 및 전망에 대해 설명하였다.

• Corrosion Science and Technology
• /
• 제17권2호
• /
• pp.45-53
• /
• 2018

A new 80Ti-15Ta-5Zr wt% alloy surface was protected by anodic oxidation in phosphoric acid solution. The protective oxide layer (TiO2, ZrO2 and Ta suboxides and thickness of 15.5 nm) incorporated $PO{_4}^{3-}$ ions from the solution, according to high resolution XPS spectra. The AFM analysis determined a high roughness with SEM detected pores (20 - 50 nm). The electrochemical studies of bare and anodically oxidized Ti-15Ta-5Zr alloy in Carter-Brugirard saliva of different pH values and saliva with 0.05M NaF, pointed to a nobler surface for the protected alloy, with a thicker electrodeposited oxide layer acting as a barrier against aggressive ions. The oxidized alloy significantly decreased corrosion current densities and total quantity of ions released into the oral environment in comparison with the bare one, at higher polarisation resistance and protective capacity of the electrodeposited layer. The impedance data revealed a bi-layered oxidation film formed by: a dense, compact, barrier layer in contact with the metallic substrate, decreasing the potential gradient across the metal/oxide layer/solution interface, reducing the anodic dissolution and a more permissive, porous layer in contact with the electrolyte. The open circuit potential for protected alloy shifted to nobler values, with thickening of the oxidation film signifying long-term protection.

• 한국수산과학회지
• /
• 제35권4호
• /
• pp.451-453
• /
• 2002

The rotation of the flagellar motor is powered by the electrochemical gradient of specific ions across the cytoplasmic membrane. Recently, the gents of the Na'-driven motor have been cloned from marine bacterium of Vibrio sp. and some of the motor proteins have been purified and characterized. Also, motx gene encoding a channel component of the sodium type flagellar motor was identified from Vibrio Huuiaiis (KTCC 2473). The amino acid sequence of MotX protein from V, Huvialis shared 90, 85, $85\%$ identity with V, cholerae, V. alginolyticus, V parahaemolyticus, respectively. We have studied the localization of the expressed MotX protein in Escherichia coli by immune-gold labeling of ultra-thin frozen section. Our observation of the expressed protein indicated that MotX protein could be existed as attachment to inner membrane in E. coli.