• 생약학회지
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• 제16권2호
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• pp.93-98
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• 1985

This investigation was performed to study the effect of Ginseng water extract on the cardiac sarcolemma $Na^+,\;K^+-ATPase$ activity of rat hearts. The Ginseng water extract (100mg/kg/day) was administered orally to Sprague-Dawley rats for one, four and seven days. The fragment of sarcolemma was prepared by the method of Matsui and Erdmann and the $Na^+,\;K^+-ATPase$ and $Mg^{++}-ATPase$ activity were measured by the method of Martins and Doty. $Na^+,\;K^+-ATPase$ activity in the rat heart treated with Ginseng water extract for 1 day was not significantly different from control value, but the activity was decreased by 13.4% in the rat heart treated for 4 days and was decreased by 20.4% in the 7 days treated group. $Mg^{++}-ATPase$ activity in the rat treated with ginseng water extract was similar to control value. It may be concluded that chronic administration of Ginseng may inhibit the $Na^+,\;K^+-ATPase$ enzyme activity, but single administration may not inhibit the activity.

• 대한약리학회지
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• 제6권1호
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• pp.1-7
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• 1970

The effects of ouabain and diphenylhydantoin on ATPase activity in rat erythrocyte membranes were studied and also influence of K on ATPase activity was studied. The ATPase activity of rat erythrocyte membrane has been shown to consist of two components. The first component requires the Mg but occurs in the absence of Na or K (Mg-ATPase) and is not inhibited by ouabain and stimulated by diphenylhydantoin. The second component requires the presence of Mg and also Na or K (Na-K-Mg-ATPase). It is inhibited by ouabain and is stimulated by diphenylhydantoin in low Na concentration and inhibited in high Na concentration. K inhibit Na-K-Mg-ATPase which is inhibited by ouabain. Ouabain and diphenylhydantoin show reversed effect to Na-K-Mg-ATPase activity. It suggest that the therapeutic effect of diphenylhydantoin on digitalis induced cardiac arrhythmia may be resulted from their effect on ion transport mechanism of cell membrance. And the relevance of these findings to the action of ouabain and diphenylhydantoin on membrane transport mechanism is discussed.

• Environmental Analysis Health and Toxicology
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• 제9권1_2호
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• pp.1-8
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• 1994

Nerve conduction impairment in lead neuropathy has been empirically linked to altered nerve myo-inositol metabolism. In most cases of neuropathy, abnormal myo-inositol metabolism is associated with abnormal $Na^+/K^+$ATPase provides a potential mechanism to relate defects of the myo-inositol metabolism in the peripheral nerve treated with lead. Therefore, the effect of lead on the rat sciatic nerve $Na^+/K^+$ATPase and other ATPase of sciatic nerve was studied. ATPase activity was measured enzymatically in sciatic nerve homogenates from 2-wk lead treated neuropathy rats and age-mached controls administered myo-inositol. $Na^+/K^+$ATPase components were assessed by ouabain inhibition or the omission of sodium and potassium ions. Lead reduced 50% reduction in the $Na^+/K^+$ATPase activity in homogenates of sciatic nerve. The 50% reduction in the $Na^+/K^+$ ATPase activity was selectively prevented by myo-inositol treatment. This study suggests that the toxic mechanism of the lead on peripheral nerve may be through reduction in $Na^+/K^+$ATPase activity which has been linked to axonal transport slowing in the rat model of lead neuropathy, via direct changes by the perturbation of the intracelluar sodium or potasium level.

• 대한약리학회지
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• 제2권2호
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• pp.35-42
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• 1966

The author investigated the effect of $Mg^#$, $Ca^#$, $Na^+$, $K^+$ and creatine phosphate on the ATPase activity of microsomal fraction isolated from rabbit uterus and obtained the following results : 1) The uterine microsomal fraction contained the $Na^+-$ and $K^+-$ activated ATPase in the presence of $Mg^#$. The ATPase activity increased with protein content in the fraction. 2) The maximum ATPase activity was obtained at $Na^+$ and $K^+$ concentraction of 100 mM respectively. 3) In the absence of $Mg^#$, the ATPase was not activated by $Na^+$ and $K^+$, but inhibited. 4) Car stimulated the $Na^+-$ and $K^+-$ activated ATPase in the presence of $Mg^#$. However, in the absence of $Mg^#$, the ATPase was not activated by $Ca^#$. 5) The $K^+-$ activated ATPase activity was greater than the $Na^+-activated$ ATPase under all conditions. 6) The $Na^+-$ and $K^+$ activated ATPase activity was increased by addition of creatine phosphokinase and creatine phosphate to the reaction mixture.

• The Korean Journal of Physiology
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• 제17권2호
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• pp.161-168
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• 1983

Studies on the effects of vanadate for Na-K-ATPase activity were carried out with rabbit renal cortex. 1) Na-K-ATPase activity was inhibited with the concentrations of vanadate in incubation medium. The vanadate concentration at which activity was inhibited by 50%$(ID_{50})$ was $10^{-6}M$ and Hill coefficient was 1.00. 2) The fractional inhibition by constant concentration of vanadate decreased with increasing enzyme concentration. 3) Increasing $K^+$ and $Na^+$ concentrations in incubation medium diminished the ability to inhibit Na-K-ATPase by vanadate whereas increasing $K^+$ and $Mg^{2+}$ concentrations potentiated the inhibition of Na-K-ATPase by vanadate. 4) Vanadate didn't inhibit Na-K-ATPase at pH 6.6. Increasing pH potentiated the inhibition of Na-K-ATPase activity. 5) Vanadate inhibited Na-K-ATPase activity reversibly in all range of concentrations in dilution experiment. These results show that vanadate inhibits Na-K-ATPase activity with interacting at $KE_2$ state reversibly.

• The Korean Journal of Physiology
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• 제1권2호
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• pp.141-150
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• 1967

The present investigation was initially undertaken to see if there exists $Na^+-K^+$ activated ATPase in the microsome fraction of the kidney. Having confirmed the presence of such an enzyme, further attempts have been made to characterize its nature and the following conclusions were obtained: (1) The ATPase activity was greatest at the $Na^+$ concentration of 100 mM as well as at $K^+$ concentration of 10 mM. Moreover, the ATPase activity was found to be depressed by $Ca^{++}$ in the presence of $Mg^{++}$. (2) While the ATPase activity was depressed by Ouabain, the magnitude of inhibition was greater in the Na medium than in the K medium. (3) NaCN augmented the ATPase activity whereas NaF and IAA depressed it. On the other hand, DNP had little influence on the ATPase activity. (4) Diamox, vasopressin and aldosterone had no effect while $HgCl_2$ markedly depressed the ATPase activity These findings indicate that the nature of ATPase isolated from the microsome fraction of the rabbit kidney is quite similar to that from other organs such as the heart and the muscle, although there are certain features specific to the type of organs.

• 한국식품영양학회지
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• 제10권2호
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• pp.151-159
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• 1997

근원섬유단백질의 이온강도에 따른 Ca-ATPase 활성, Mg-ATPase 활성 및 EDTA-ATPase 활성은 오징어와 대합에서 그 차이점이 뚜렷하였으며, activity-pH curve에서 오징어 actomyosin의 Ca-ATPase 활성은 biphasic response가 소실되었고 대합의 actomyosin은 미약한 bipasic response가 나타났다. 또한 저농도의 dioxane에 의하여 오징어의 근원섬유단백질은 급격한 활성의 감소를 보였으나 대합의 근원섬유단백질은 활성이 증가되었다. 그리고 에탄올과 메탄올은 오징어와 대합의 myosin 및 MM에 대하여 저농도에서 활성을 증가시켰다. 한편 NEM으로 근원섬유단백질을 modification시키며 10-6M 이하의 NEM 농도에서는 활성이 증가되었으나 10-5M 이상의 농도가 되면 활성의 급격한 감소가 나타났다.

• 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.

• The Korean Journal of Physiology
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• 제10권1호
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• pp.25-34
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• 1976

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

• Applied Biological Chemistry
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• 제48권3호
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• pp.212-216
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• 2005

Thapsigargin은 동물조직에서 ER/SR-type $Ca^{2+}-ATPase$의 선택적 저해제로서, 토마토 뿌리조직으로부터 분리한 마이크로솜에서 ATPase의 특성을 조사하기 위하여 사용되었다. Thapsigargin은 마이크로솜 ATPase 활성을 농도의존적으로 저해하였으며, $10\;{\mu}M$ 농도에서 총활성의 약 30%를 저해하였다. 이것은 뿌리조직에서 $Ca^{2+}-ATPase$의 활성이 매우 낮다는 것을 고려할 때, thapsigargin이 뿌리조직의 주된 ATPase 활성인 원형질막 및 액포막의 $H^+-ATPase$ 활성을 저해할 가능성을 보인다. Thapsigargin의 효과는 ${NO_3}^-$를 사용하여 액포막 $H^+-ATPase$ 활성을 저해하였을 때 현저하게 감소하였다. 그러나, thapsigargin의 효과는 원형질막의 $H^+-ATPase$ 활성에는 영향을 미치지 않아, thapsigargin이 토마토 뿌리조직에서 액포막 $H^+-ATPase$를 선택적으로 저해함을 보여준다.