• 한국동물학회지
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• 제38권4호
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• pp.449-456
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• 1995

북방산개구리 뇌 조직의 Na+, K+, ATPase와 Mg2+-ATPase 활성도와 특성의 계절에 따른 변화를 연구하였다. 북방산개구리 뇌에서 Na+, K+, ATPase 활성도는 활동기와 동면기에 비슷한 활성도를 나타내고, 동면에서 깨어나는 각성기와 동면으로 들어가는 시기에 높은 활성도를 나타내었다. 5-35$^{\circ}C$의 온도에서 각 계절 전반에 걸쳐서 Na+, K+, ATPase는 non-linear Arrhenius kinetics를 보였다. Mg2+-ATPase는 동면기에 분명하게 감소하였으며 각성기에는 뚜렷하게 증가하였다. Mg2+-ATPase는 모든 계절에 걸쳐서 linear Arrhenius kinetics를 나타내었다. Na+, K+, ATPase의 15$^{\circ}C$/35$^{\circ}C$에서 활성도의 비에는 동면기와 활동기에 유의성 있는 차이가 나타나지 않았다. ouanain에 의한 Na+, K+, ATPase의 활성 저해 양상도 계절에 따른 변화가 없었다. 본 결과는 동면기에도 활동기와 마찬가지로 개구리 뇌의 Na+, K+, ATPase의 생화학적 특성과 활성도가 유지됨을 시사한다.

• 한국동물학회지
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• 제17권2호
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• pp.93-102
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• 1974

토끼의 골격근 小胞體 切片을 遠心分離하여 그 ATPase 活性의 生化學的性質을 $Mg^++ - ATPase 와 (Mg^++ - Ca^++)$-ATPase로 구분하여 조사하였다. $(Mg^++ - Ca^++)$-ATPase의 活性은 $0^\\circ - 40^\\circ C$의 범위, 그리고 pH 6.4-7.6의 범위에서는 $Mg^++$-ATPase보다 훨씬 높다. 이 현상은 온도가 높을수록 더욱 현저하다. 活性化에너지는 온도 $0^\\circ -40^\\circ C$의 범위에서는 $Mg^++$-ATPase가 14kcal/mole, $(Mg^++ - Ca^++)$-ATpase 가 21kcal/mole, 그리고 total ATPase 가 18kcal/mole 이다. 이 活性化에너지의 값은 pH와 Mg 濃度에 무관하다. 이들 효소의 Km의 값은 $Mg^++$-ATPase 가 0.36mM , $(Mg^++ - Ca^++)$-ATpase가 2.20mM, 그리고 total ATPaserk 0.86 mM이다.

• 대한소아치과학회지
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• 제10권1호
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• pp.139-147
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• 1983

This study was undertaken to evaluate the physiological roles & mechanism of $Ca^{++}$-ATPase & $Mg^{++}$-ATPase in human dental pulp. Each specimen of dental pulp was obtained from the freshly extracted, freeze-dried 242 teeth. $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were measured by the release of inorganic phosphate & protein with Spectrophotometer. The results were as follows; 1. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significantly increased in developing teeth. 2. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significantly decreased in nonvital teeth. 3. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significant decreased in deciduous teeth. 4. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity didn't have relation with dental caries. 5. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase were activated by either $Ca^{++}$ alone or $Mg^{++}$ alone.

• The Korean Journal of Physiology
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• 제10권2호
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• pp.1-10
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• 1976

The action of acetylcholine 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 acetylcholine on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is inhibited by acetylcholine. 2. The ratio of inhibition of NaK ATPase by acetylcholine is decreased by raising the potassium concentration, and is increased by raising the sodium concentration. 3. The ATPase activity is increased by small amounts of calcium but inhibited by larger amounts. The ratio of inhibition of the enzyme by acetylcholine is increased by raising the calcium concentration. 4. The inhibitory action of acetylcholine on the NaK ATPase activity was not related to the sulfhydryl group of cysteine, the hydroxyl group of threonine, or the carboxyl group of aspartic acid. 5. The inhibitory action of acetylcholine on the ATPase activity is due to amino group of the enzyme of NaK ATPase.

• 대한한의학회지
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• 제18권1호
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• pp.198-207
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• 1997

To explore the action mechanism of Ijintang in the brain, the authors investigated the effects of Ijintang fractions on MgNaK ATPase and MgCa ATPase in rat brain synaptosomes prepared from cerebral cortex. The activities of MgNaK ATPase and MgCa ATPase were assayed by the level of inorganic phosphate liberated from the hydrolysis of ATP. Fraction WH-95-7 at the concentration of $10^{-2}%$ decreased the activity of MgNaK ATPase about 34.1% and also reduced the activity of MgCa ATPase about 49.3% But, other fractions (WB-95-7, WC-95-7, MB-95-7, MC-95-7, MH-95-7) did not significantly changed the activities of the MgNaK ATPase and MgCa ATPase The decreased activity of MgNaK ATPase by WH-95-7 will decrease the rate of $Ca^{2+}$ efflux, probably via an Na-Ca exchange mechanism and will increase the rate of $Ca^{2+}$ entry by the depolarization of nerve terminals. The reduced activity of MgCa ATPase by WH-95-7 will result in the decreased efflux of $Ca^{2+}$. As a conclusion, it can be speculated that lithium elevates the intrasynaptosomal $Ca^{2+}$ concentration via inhibition of the activities of MgNaK ATPase and MgCa ATPase. and this increased $[Ca^{2+}]i$ will cause the release of neurotransmitters.

• 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.

• 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.

• The Korean Journal of Physiology
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• 제6권1호
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• pp.27-31
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• 1972

The activity of Mg and Na-K activated ATPase of homogenate from rat brain cortex was measured in vitro under the variety of conditions. The effects of various hypnotic and tranquilizer such as phenobarbital, amobarbital, diazepam, promazine and chlorpromazine on the activities of both ATPase was investigated and the results was summarized as follows. 1. Na-K ATPase was slightly inhibited by phenobarbital and amobarbital while Mg ATPase was moderately activated by these drugs. 2. Both Mg and Na-K ATPase activities were markedly inhibited by diazepam. 3. Promazine and chlorpromazine markedly inhibited both Mg and Na-K ATPase activities. These findings indicate that remarkable correlation between hypnotic or tranquilizing potency and ATPase inhibition could be observed.

• 약학회지
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• 제22권3호
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• pp.120-127
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• 1978

We have studied the effect of ouabain, tool ginseng saponin, panax saponin C (protopanaxatriol derivative) and ginsenoside $Rb_{1}$ (protopanaxadiol derivative) on $Na^+,K^+$-ATPase and $Mg^{++}$-ATPase activities were determined by the method of Robinson and ATPase activities were determined by the method of King. The $Na^+,K^+$-ATPase activities were inhibitied by 90.1% and 51.1% respectively at the concentration of $10^{-3}M$ and $10^{-4}M$ ouabain. The results are consistent with those of Robinson. The $Na^+,K^+$-ATPase activities were increased by 14.3% and 10.0% respectively at the concentration of $10^{-4}$g/ml and $10^{-5}$g/ml total ginseng saponin. Panax saponin C obtained by the method of Han and ginsenoside $Rb_{1}$ obtained by the method of Shibata were used. The $Na^+,K^+$-ATPase activities were increased in the presence of panax saponin C and the increased activity with panax saponin C was greater than that with total ginseng saponin. On the other hand ginsenoside $Rb_{1}$ showed an inhibitory effect on $Na^+,K^+$-ATPase. Total ginseng saponin, panax saponin C and ginsenoside $Rb_{1}$ had no effect on $Mg^{++}$-ATPase. Therefore, it may be concluded that total ginseng saponin has dual effects on microsomal $Na^+,K^+$-ATPase, that is, panax saponin C exhibits stimulatory action, whereas ginsenoside $Rb_{1}$ shows inhibitory action.

• 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.