Reverse electrodialysis (RED) is green energy technologies to produce electric power using the salinity gradient. The salinity gradient generates chemical potential difference by transport of ions through the membranes. In RED system, anion exchange membrane (AEM) and cation exchange membrane (CEM) play a major role in transporting cation (Na+) and anion (Cl-), respectively. Significant technical issue is how to enhance conductivity and permselectivity of membrane simultaneously in the system. In this study, we characterized influences of cationic functional groups on AEM. We evaluated conductivity and permselectivity of AEM introduced three types of cationic salt functional groups.

Na+/K+-ATPase is a membrane protein and plays a key role in osmotic regulation in living organisms. In the present study, a cDNA sequence encoding the Na+/K+-ATPase alpha subunit from the monogonont rotifer, Brachionus koreanus was cloned by rapid amplification of cDNA ends technique. To investigate the role of this enzyme in osmotic stress, enzymatic activities of Na+/K+-ATPase were measured after exposure to different salinities for 48 h. The full-length Bk Na+/K+-ATPase cDNA was 3069 bp-long, encoding a 1022-amino acid polypeptide. Bk Na+/K+- ATPase possesses eight membrane spanning regions and five conserved domains. Phylogenetic analysis showed that Bk Na+/K+-ATPase had high identity with those of other species, and was closely clustered with other Brachionus sp. These findings indicate that this protein was conserved both structurally and functionally. B. koreanus Na+/K+-ATPase activity was stimulated in both hyposaline (6 psu) and hypersaline (32 psu) conditions, suggesting that this protein may play a role in osmoregulation. This study would provide better understanding of the physiology of B. koreanus and this enzyme may be useful as a molecular marker for evaluation of osmotic stress in aquatic environment.

Na+/K+-ATPase, an energy-transducing ion pump, is responsible for maintenance of relatively high concentrations of potassium ions but low concentrations of sodium ions in the cell by transport of these ions across the plasma membrane and participates in transport of various nutrients including glucose, amino acids. and ions. Na+/K+-ATPase consists of α, β, and FXYD subunits, but only α and β subunits are needed for basic functions. FXYD subunit is an auxiliary protein for αβ complex of Na+/K+-ATPase. Our recent study has shown that α (ATP1A1-4) and β (ATP1B1-3) subunits of Na+/K+-ATPase are expressed in the uterine endometrium during the estrous cycle and pregnancy in pigs. In this study, we further determined expression of FXYD (FXYD1-7) subunits of Na+/K+-ATPase in the uterine endometrium during the estrous cycle and pregnancy in pigs. Real-time RT-PCR analysis showed that mRNAs for all subtypes of FXYD subunit were expressed in the uterine endometrium during the estrous cycle and pregnancy in a pregnancy status- and stage-specific fashion. In situ hybridization analysis exhibited that transcripts of all subtypes of FXYD subunit were primarily localized to luminal (LE) and glandular epithelia (GE) during the estrous cycle and early pregnancy and to chorionic membrane (CM) during mid to term pregnancy. RT-PCR analysis showed that FXYD subunits were expressed in conceptuses on D12 and D15 of pregnancy. These results indicate that all subtypes of FXYD subunit are expressed in the uterine endometrium and conceptuses during the estrous cycle and pregnancy in a pregnancy status- and stagespecific manner. These suggest that FXYD may be involved in the establishment and maintenance of pregnancy by regulating the activity of Na+/K+-ATPase in nutrient transport at the maternal-fetal interface in pigs. * This work was supported by the Next Generation BioGreen 21 program (#PJ007997), RDA and the National Research Foundation (NRF #2010-0012304) funded by the Korean Government, Republic of Korea.

Na+/K+-ATPase, an energy-transducing ion pump, is responsible for maintenance of relatively high concentrations of potassium ions but low concentrations of sodium ions in the cell by transport of these ions across the plasma membrane. Na+/K+-ATPase consists of α, β, and γ subunits, but only α and β subunits are needed for basic functions. Na+/K+-ATPase is also involved in regulation of intracellular calcium ion concentration by coupling with Na+/Ca2+ exchanger involved in intracellular calcium extrusion. Our previous study showed that calcium regulatory molecules including Na+/Ca2+ exchanger are expressed in the uterine endometrium during the estrous cycle and pregnancy in pigs, however, expression of Na+/K+-ATPase in the uterine endometrium has not been determined. Thus, we examined expression of α1 (ATP1A1) and β1 (ATP1- B1) subunits of Na+/K+-ATPase in the uterine endometrium during the estrous cycle and pregnancy in pigs. Real-time RT-PCR analysis showed that levels of ATP1A1 m- RNA in the uterine endometrium during the estrous cycle and early pregnancy were higher than those during mid and term pregnancy, and that levels of ATP1B1 mRNA were highest on day (D) 12 of the estrous cycle. In situ hybridization analysis revealed that ATP1A1 and ATP1B1 mRNAs were localized to luminal (LE) and glandular epithelia (GE) in the endometrium. During mid to term pregnancy, localization of ATP1A1 mRNA was confined to LE, GE, and chorionic membrane (CM) of areolae and ATP1- B1 mRNA was localized to LE, GE and CM with the strongest intensity in LE of areolae. Signal intensity of ATP1B1 mRNA in LE was slightly stronger than that in GE. RT-PCR analysis showed that ATP1A1 and ATP1B1 mRNAs were expressed in conceptuses on D12 and D15 of pregnancy. These results showed that ATP1A1 and ATP1B1 were expressed in the uterine endometrium and conceptuses during the estrous cycle and pregnancy in a pregnancy status- and stage-specific manner. These suggest that Na+/K+-ATPase may play a key role in the establishment and maintenance of pregnancy by regulating intracellular concentrations of various ions including calcium at the maternal-fetal interface in pigs.

Na+ ion conductivity can be improved by the substitution of an Mg atom for an Al atom to form a nonstoichiometric Na+ β-alumina. We performed a first principles study to investigate the most stable substitution site of an Mg atom and the resulting structural change of the nonstoichiometric Na+ β-alumina. Al atoms were classified as four different layers in the spinel block that are separated by conduction planes in the nonstoichiometric Na+ β-alumina. The substitution of an Mg atom for an Al atom at a tetragonal site was more favorable than that at an octahedral site. The substitution in the spinel block was more favorable than that close to the conduction plane. This result was well explained by the volume changes of the polyhedrons, by the standard deviation of the Mg-O distance, and by the comparison with bulk MgO structure. Our result indicates that the most preferable site for the Mg atom was the tetrahedral site at the spinel block in the nonstoichiometric Na+ β-alumina.

이온교환 용액내 Na+ 이온의 몰농도 증가에 따른 zeolite A의 Sr2+ 이온교환 특성을 연구하기 위하여, Sr2+ 및 Na+ 이온으로 교환된 4개의 zeolite A 단결정을 혼합 이온교환 용액을 이용하여 회분법으로 준비하였 다. 이들 이온교환용액의 전체 몰농도는 0.05M이며, Sr(NO3)2:NaNO3 몰비는 각각 1:1(crystal 1), 1:100(crystal 2), 1:250(crystal 3), and 1:500(crystal 4) 이다. 이들 단결정은 623 K와 1×10-4 Pa의 진공하에서 2 일간 탈수 시 켰다. 이들의 구조는 단결정 싱크로트론 X-선 회절법으로 입방공간군 Pm3-m을 사용하여 해석하였으며 crystals 1, 2, 3 및 4의 최종 오차 인자를 각각 0.047/0.146, 0.048/0.142, 0.036/0.128, and 0.040/0.156로 정밀화하였다. Crystal 1과 2에서는 6개의 Sr2+ 이온이 결정학적으로 서로 다른 3개의 위치에서 발견되었다. Crystal 3에서는 1 개의 Sr2+ 이온과 10개의 Na+ 이온이 large cavity와 sodalite 내부에서 발견 되었다. Crystal 4 에서는 단지 12 개의 Na+ 이온만이 3개의 서로 다른 결정학적 자리에 점유하고 있었다. Sr2+ 이온의 이온교환율은 초기 Na+ 이온의 농도가 증가하고 Sr2+ 이온의 농도가 감소함에 따라 100에서 16.7 및 0%로 급격하게 감소 하였다. 또한, Sr2+ 이온 교환률이 감소 함에 따라 제올라이트 골격의 단위 격자 상수 값이 갑소 하였다.

본 논문에서는 고에너지 엑스선(6MeV)을 조사한 세포막 모델에서 K+-Na+ pump 시스템의 능동적 전달특성에 대하여 연구하였다. 이 실험에 사용된 세포막 모델은 Na+슬폰화 폴리스티렌-디비닐벤젠(polystyrene-divinylbenzene) 혼성 중합막을 사용하였다. 이온의 초기플럭스는 H+이온 농도의 증가와 함께 증가하였다. 이 실험의 조건을 pH 1.5-5, 온도 36.5℃로 하여 첫 번째, 방사선이 조사되지 않은 막에서 K+의 초기플럭스는 2.09x10-4-1.32x10-3mole/cm2·h이고 Na+의 초기플럭스는 7.09 x10-4-1.09x10-3mole/cm2·h으로 나타내었다. 두 번째, 방사선이 조사된 막에서 K+의 초기플럭스는 21.0x10-4-16.7x10-3mole/cm2·h이고 Na+의 초기플럭스는 62.0x10-4-20.6x10-3mole/cm2·h으로 나타내었다. 막의 K+/Na+선택도는 약 1.10이다. 조사된 막의 pH의 추진력은 조사되지 않은 막보다 약 9-20배 정도 유의성 있게 증가하였다. 세포막모델에서 K+-Na+의 pump 시스템의 능동적 전달특성이 비정상적이기 때문에 세포장해가 세포에서 발현된다고 사료된다.

The adsorption of lithium ion onto zeolite was investigated depending on contact time, initial concentration, cation forms, pH, and adsorption isotherms by employing batch adsorption experiment. The zeolite was converted into different forms such K+, Na+, Mg2+, Ca2+, and Al3+. The zeolite had the higher adsorption capacity of lithium ion in K+ form followed by Na+, Ca2+, Mg2+, and Al3+ forms, which was in accordance with their elctronegativities. The lithium ion adsorption was explained using the Langmuir, Freundlich, and Dubinin-Radushkevich adsorption isotherms and kinetic models. Adsorption rate of lithium ion by zeolite modified in K+ form was controlled by pseudo-second-order and particle diffusion kinetic models. The maximum adsorption capacity obtained from Langmuir isotherm was 17.0 mg/g for zeolite modified in K+ form. The solution pH influenced significantly the lithium ions adsorption capacity and best results were obtained at pH 5-10.

Na+/K+-ATPase, an energy-transducing ion pump, is responsible for maintenance of relatively high concentrations of potassium ions but low concentrations of sodium ions in the cell by transport of these ions across the plasma membrane and participates in transport of various nutrients including glucose, amino acids, and ions. In addition, Na+/K+-ATPase is also involved in regulation of intracellular calcium ion concentration by coupling with Na+/Ca+ exchanger expressed at the maternal-fetal interface in pigs. Na+/K+-ATPase consists of α, β, and FXYD subunits, but only α and β subunits are required for primary functions. FXYD subunit is an auxiliary protein for αβ complex of Na+/K+-ATPase. However, it has not been determined that subunits of Na+/K+-ATPase are expressed in the uterine endometrium during the estrous cycle and pregnancy in pigs. In this study, we determined expression of alpha (ATP1A1-4), beta (ATP1B1-3), and FXYD (FXYD1-7) subunits of Na+/K+-ATPase in the uterine endometrium during the estrous cycle and pregnancy in pigs. Real-time RT-PCR analysis showed that all alpha, beta, and FXYD subunits, except ATP1A3, were expressed in the uterine endometrium during the estrous cycle and pregnancy in a pregnancy status- and stage-specific fashion. In situ hybridization analysis exhibited that ATP1A1, ATP1A4, and ATP1B1 were localized to luminal (LE) and glandular epithelium (GE) during the estrous cycle and early pregnancy, and during mid to term pregnancy. ATP1A1 mRNA was localized to LE, GE, and areolae of the chorioallantois, especially at high levels to LE in areolae regions. ATP1B3 mRNA was detected only in LE during the estrous cycle and pregnancy with highest levels on day (D) 12 of pregnancy. Transcripts of all subtypes of FXYD subunit were primarily localized to LE and GE during the estrous cycle and early pregnancy and to chorionic membrane (CM) during mid to term pregnancy. RT-PCR analysis showed that all subtypes of Na+/K+-ATPase subunits, except ATP1A2, ATP1A3, and ATP1B2 mRNAs, were expressed in conceptuses on D12 and D15 of pregnancy. These results indicate that Na+/K+-ATPase subunits are expressed in the uterine endometrium and conceptuses during the estrous cycle and pregnancy in a pregnancy status- and stage-specific manner. These suggest that Na+/K+-ATPase subunits may be involved in the establishment and maintenance of pregnancy by coordinate regulation of absorption and secretion of nutrients such as glucose, amino acids, and ions at the maternal-fetal interface in pigs.