• Ocean and Polar Research
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• 제34권2호
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• pp.137-149
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• 2012

남해의 광양만과 진해만에 서식하는 자연산 참굴의 건강성 평가를 위해 세포성 면역을 담당하는 혈구의 기능들을 유세포 분석기와 Neutral Red Retention(NRR) assay를 이용하여 신속, 정확하게 측정하였다. 광양만과 진해만의 안쪽과 바깥쪽에 서식하는 자연산 참굴의 혈구를 유세포 분석기를 이용하여 형태학적 특성에 따라 혈구의 종류를 분류하고, 혈구 종류별 수, 사멸률, DNA 손상도, 식세포능을 측정하였다. 또한 NRR assay를 이용하여 혈구의 lysosomal membrane stability를 측정하였다. 참굴의 혈구는 granulocytes, hyalinocytes, blast-like cells의 세 가지 종류로 분류되었다. 조사 지역 간의 혈구의 수, 사멸률, DNA 손상도는 유의적 차이가 없었지만, 식세포율과 lysosomal membrane stability와 같은 면역 관련 기능들은 유의적 차이가 있었다. 진해만은 내만과 외만 지역에 서식하는 참굴의 혈구 면역인자들 간에는 유의적 차이가 관찰되지 않았다. 이에 반해, 광양만에 서식하는 참굴은 내만 지역의 섬진대교가 외만 지역의 평산리 지역에 서식하는 참굴보다 낮은 식세포율과 낮은 lysosomal membrane stability를 보여 면역력이 저하되어 있는 것으로 추정된다. 하지만, 해양환경 변화와 시료의 면역력과의 상관관계를 이해하기 위해서는 조사지역의 환경적 특성이나 오염정도, 그리고 시료 내의 오염물질 축적량 등의 객관적인 분석 결과와의 종합적인 고찰이 필요할 것이다. 유세포 분석기와 NRR assay를 이용한 참굴 혈구 집단의 형태 변화 및 면역능 측정 기술은 시료의 전처리 없이 빠른 시간 내에 세포의 특성을 분석할 수 있는 유용한 분석 tool로 활용될 수 있음을 확인하였다.

• 접착 및 계면
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• 제24권1호
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• pp.17-25
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• 2023

본 연구는 투명 폐 Polyethylene Terephthalate (PET)병을 재활용하여 지지체를 제조 후에 Polyetherimide (PEI)를 이용하여 친환경적인 유기용매나노여과막 (Organic Solvent Nanofiltration)에 이용하고자 하였다. 제조된 복합막은 먼저, PET 지지체는 전기방사를 통해 제조를 하였으며 이후 내용매성이 우수한 PEI를 이용하여 지지체 위에 캐스팅하였고 비용매 유도상분리(Non-solvent Induced Phase Separation, NIPS) 방법을 이용하여 유기용매나노여과막을 제조하였다. 먼저 막제조에 앞서 제조된 PET 지지체는 모폴로지 분석을 통해 섬유의 직경과 인장강도를 파악하였으며 유기용매나노여과막의 최적 지지체 조건을 확인하였다. 이후 제조된 PET/PEI 복합막은 PEI의 농도에 따른 유기용매나노여과막으로서의 성능을 파악하기 위하여 에탄올에 분자량 697 g/mol을 가지는 Congo red의 제거율을 확인하였으며 최종으로 Congo red의 제거율이 90%이상의 제거율을 가지는 최적의 PET/PEI 복합막을 확인하였다.

• The Korean Journal of Physiology
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• 제23권1호
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• pp.13-21
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• 1989

The present study was designed to investigate i) the action of various nucleotides on membrane permeability of rat red blood cell and hepatocyte for $Na^{+}$ and $Rb^{+}$ ii) the characteristics of purinoceptors on these cell membranes. Blood from Sprague-Dawley rats was obtained by carotid arterial cannulation. Red blood cells were then washed 3 times with saline at $4{\circ}C$. Hepatic parenchymal cells were isolated from rat livers by using a modification of the Berry and Friend (1969) method. For the $Na^{+}$ influx studies, isolated RBC and hepatocyte were incubated in incubation medium containing $^{22}Na^{+}0.2\;{\mu}Ci/ml$ at $37^{\circ}C$. After various time intervals samples were removed from the incubation flask and washed out 3 times with ice-cold washing solutions. Cells were destroyed by adding Triton X-100 and TCA solution. After centrifugation, the supernatants were assayed for $^{22}Na^{+}$ by gamma counter. $^{86}Rb^{+}$ was used to simulate $K^{+}$ in these $K^{+}efflux$ studies. Isolated hepatocytes were incubated for 60 min in the loading solution containing $^{86}Rb^{+}\;10\;{\mu}Ci/ml$ at $37^{\circ}C$. After loading, the cells washed out 3 times by centrifugation with washing solution. The cells were incubated in buffer solution at $37^{\circ}C$. At intervals thereafter, samples were removed and centrifuged. The supernatants were analyzed for $^{86}Rb^{+}$ by liquid scintillation counter. The main results of the experiments were: 1) ATP and ATPP increased in both $^{22}Na^{+}$ influx and $^{86}Rb^{+}$ efflux in the red blood cell. Although ADP showed a tendency to increase in RBC membrane permeability for $^{22}Na^{+}$ and $^{86}Rb^{+}$, the changes were not significantly different from the control. 2) The Significant changes in $^{22}Na^{+}$ and $^{86}Rb^{+}$ flux by ATP were also demonstrated in hepatocyte. ATPP and ADP showed a tendency to increase in hepatocyte membrane permeability for both ions. 3) Other nucleoside triphosphates-ITP, GTP and CTP-did not change in membrane permeability for $^{22}Na^{+}$ and $^{86}Rb^{+}$ in RBC and hepatocyte. In conclusion, not only ATP but also ATPP activate purinoceptors and change in membrane permeability for $Na^{+}$ and $K^{+}$. In order to activate purinoceptors on the cell membrane, the nucleotides have to possess intact adenine moiety and three phosphates or more in its molecule.

• 한국막학회:학술대회논문집
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• 한국막학회 2004년도 Proceedings of the second conference of aseanian membrane society
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• pp.55-58
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• 2004

Cell separation from peripheral blood was investigated using surface-modified polyurethane (PU) membranes with different functional groups. Both red blood cells and platelets could pass through unmodified PU and PU-SO$_3$H membranes, while the red blood cells preferentially passed through PU-N(C$_2$H$_{5}$ )$_2$ and PU-NHC$_2$H$_4$OH membranes. The permeation ratio of T and B cells was less than 25% for the surface-modified and unmodified PU membranes. CD34$^{+}$ cells have been recognized as various kinds of stem cells including hematopoietic and mesenchymal stem cells. The adhesiveness of CD34$^{+}$ cells on the PU membranes was found to be higher than that of red blood cells, platelets, T cells or B cells. Overall, the adhesiveness of blood cells on the PU membranes increased in the following order: red blood cells $\leq$ platelets ＜ T cells $\leq$ B cells ＜ CD34$^{+}$ cells. Treatment of PU-COOH membranes with a human albumin solution to detach adhered blood cells, allowed recovery of mainly CD34$^{+}$ cells in the permeate, while both red blood cells and platelets could be isolated in the permeate using unmodified PU membranes. The PU membranes showed different permeation and recovery ratios of specific cells depending on the functional groups attached to the membranes.mbranes.

• The Korean Journal of Physiology
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• 제10권1호
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• pp.15-24
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• 1976

The action of aconite on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of aconite on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is stimulated by aconite, and the concentration of aconite for maximal activity is about 80 mg%. The pH optimum for the aconite sensitive component is 8.0. 2. The activating effect of aconite on the ATPase, with a given concentration of sodium in the medium, is increased by raising the potassium concentration but activity ratio is decreased. 3. The activating effect of aconite on the ATPase, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased. 4. The action of aconite on the ATPase activity is inhibited by calcium ions and the effect of inhibition is increased by small amounts of calcium but decreased by larger amounts. 5. The activating effect of aconite on the ATPase was not related to the sulfhydryl group of cysteine, the amino group of lysine, the hydroxyl group of threonine or the imidazole group of histidine. 6. The action of aconite on the ATPase activity is due to carboxyl group of the enzyme of NaK ATPase.

• The Korean Journal of Physiology
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• 제12권1_2호
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• pp.15-23
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• 1978

The action of ascorbic acid on the sodium Plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action if ascorbic acid on the ATPase activity The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is stimulated by ascorbic acid and the concentration of ascorbic acid for maximal activity is about 8 mM. 2. The activating effect of ascorbic acid on the ATPase activaty, with a given concentration of sodium in the medium, is increased by raisins the potassium concentration but activity ratio is decreased. 3. The activating effect of ascorbic acid on the ATPase activity, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased. 4. The action of ascorbic acid on the ATPase activity is stimulated by calcium ions and activity ratio is increased by raising the calcium concentration. 5. The activating effect of ascorbic acid on the ATPase activity was not related to the sulfhydryl group of cysteine or the hydroxyl group of threonine. 6. The activating effect of ascorbic acid on the ATPase activity is due to amino group and carboxyl group of the enzyme of NaK ATPase.

• The Korean Journal of Physiology
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• 제12권1_2호
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• pp.25-34
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• 1978

The action of theobromine on the sodium plus potassium activated ATPase activity In the rabbit red cell membrane has teen investigated and the experiments were also designed to determine the mechanism of action of theobromine on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red fell membrane is stimulated by theobromine, and the concentration of theobromine for maximal activity is about 3mM. 2. The activating effect of theobromine on the ATPase, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased. 3. The activating effect of theobromine on the ATPase, with a given concentration of sodium in the medium. is increased by the raising the potassium concentration but activity ratio is decreased. 4. The NaK ATPase activity is increased by small amounts of calcium but decreased by larger amounts. The activity of the enzyme by theobromine is increased by small amounts of calcium but decreased by larger amounts. 5. The activating effect of theobromine on the ATPase was not related to the hydroxyl group of threonine and imidazole group of histicline. 6. The activating effect of theobromine on the ATPase is due to sulfhydryl group, amino group and carboxyl group of the enzyme of NaK ATPase.

• The Korean Journal of Physiology
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• 제10권1호
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• pp.1-5
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• 1976

The trypanocidal drug suramin, an impermeant polyanion, has been shown to be a powerful inhibitor of the calcium uptake and calcium-stimulated ATPase activity of sarcoplasmic reticulum (Fortes et al., 1974). In view of this finding, an attempt was made to investigate the effect of suramin on $Ca^{++}$ transport in resealed red cells and on $Ca^{++}$-activated ATPase in red blood cell membrane fragments (RBCMF). The results obtained are summarized as follows. 1. $Ca^{++}$ outflux from the resealed RBC was inhibited by suramin and the inhibitory action of suramin is proportional to the concentration of drug added inside the RBC preparation. When suramin is added both inside and outside the RBC preparation simultaneously, the magnitude of the inhibitory effect was more pronounced, suggesting that suramin inhibits both active $Ca^{++}-^{45}Ca$ exchange diffusion across the RBC membrane. 2. Suramin inhibits the $Ca^{++}$-activated ATPase of the RBCMF and the effect of inhibition by the drug was also concentration dependent. From the above results, it may be concluded that suramin inhibits $Ca^{++}$ transport across RBC membrane by inhibiting $Ca^{++}$-activated ATPase activity which has been known to be linked with active $Ca^{++}$ transport.

• The Korean Journal of Physiology
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• 제11권1호
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• pp.11-20
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• 1977

The action of pilocarpine on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of pilocarpine on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is stimulated by pilocarpine, and the concentration of pilocarpine for maximal activity is about 3 mM. The pH optimum for the pilocarpine sensitive component is 8.0. 2. The activating effect of pilocarpine on the ATPase, with a given concentration of sodium .in the medium, is increased by raising the potassium concentration but activity ratio is decreased 3. The activating effect of pilocarpine on the ATPase, with a given concentration of Potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased 4. The NaK ATPase activity is increased by small amounts of calcium but decreased by 'larger amounts. The activity ratio of the enzyme by pilocarpine is decreased by small amounts .of calcium but decreased by larger amounts. 5. The activating effect of pilocarpine on the ATPase was not related to the sulfhydryl group of cysteine, the hydroxyl group of threonine or the imidazole group of histidine. 6. The activating effect of pilocarpine on the ATPase is due to amino group and carboxyl group of the enzyme of NaK ATPase

• The Korean Journal of Physiology
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• 제11권1호
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• pp.1-9
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• 1977

Action of anthraquinone on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of anthraquinone on the ATPase activity. The following results were obtained 1. The activity of the NaK ATPase from red cell membrane is inhibited by anthraquinone and the concentration of anthraquinone for maximal inhibition is about 5mM. 2. The ratio of inhibition of NaK ATPase by anthraquinone, with a giving concentration of sodium in the medium, is increased by raising the potassium concentration. 3. The ratio of inhibition of NaK ATPase by anthraquinone, with a given concentration of potassium in the medium, is increased by raising the sodium concentration. 4. The action of anthraquinone on the NaK ATPase activity is inhibited by calcium ions and the ratio of inhibition is increased by small amounts of calcium but almost constant by larger amounts. 5. The inhibitory action of anthraquinone on the NaK ATPase activity was not related to the amino group of lysine, the hydroxyl group of threonine or the imidazole group of histidine. 6. The inhibitory action of anthraquinone on the ATPase activity is due to sulfhydryl group or the carboxyl group of the enzyme of NaK ATPase.