• Toxicological Research
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• v.5 no.2
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• pp.79-87
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• 1989

Changes in urinary $Na^+$ and $K^+$ excretions, renal cortical microsomal $Na^+$ -K-ATPase activity, cortical tissue electrolyte content and plasma aldosterone level were studied in rats treated with CdCl2 (2 mg Cd/kg/day, s.c. injection) for 7-14 days. After 7 days of cadmium exposure, urinary excretion of $Na^+$ was markedly reduced. This change was accompanied by an increase in $Na^+$-$K^+$-ATPase activity, a fall in tissue $Na^+$ content, a rise in tissue $K^+$ content and an elevation of plasma aldosterone level.

• Bulletin of the Korean Chemical Society
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• v.32 no.1
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• pp.183-185
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• 2011

Adenylate kinase-like activity and phosphotransferase-like activity from $F_1$-ATPase of Escherichia coli was revealed by $^{31}P$ NMR spectroscopy. Incubation of F1-ATPase with ADP in the presence of $Mg^{2+}$ shows the appearance of $^{31}P$ resonances from AMP and Pi, suggesting generation of AMP and ATP by adenylate kinase-like activity and the subsequent hydrolysis to Pi. Incubation of $F_1$-ATPase with ADP in the presence of methanol shows additional peak from methyl phosphate, suggesting phosphotransferase-like activity of $F_1$-ATPase. Both adenylate kinase-like activity and phosphotransferase-like activity has not been reported from $F_1$-ATPase of Escherichia coli. $^{31}P$ NMR could be a valuable tool for the investigation of phosphorous related enzyme.

• The Korean Journal of Physiology
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• v.20 no.2
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• pp.157-164
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• 1986

Since it has been reported that vanadate inhibits $Ca^{++}-ATPase$ activity without affecting $Ca^{++}$ uptake, this study was undertaken to investigate the effects of vanadate on $Ca^{++}-ATPase$ activity and $Ca^{++}$ uptake in the sarcoplasmic reticulum of rat skeletal muscle. The following results were obtained. 1) $Ca^{++}$ activated ATPase activity of the intact sarcoplasmic reticulum was significantly inhibited when vanadate was added to the incubation medium at concentration greater than $10^{-6}\;M$. However $Mg^{++}$-ATPase activity of the intact SR was not affected by vanadate at concentrations ranging from $10^{-7}\;to\;10^{-4}\;M.$ Similarly, $Ca^{++}-ATPase$ activity in sonicated sarcoplasmic reticulum was significantly reduced by vanadate at a concentration $10^{-7}$ M or higher. 2) The uptake of $Ca^{++}$ by isolated sarcoplasmic reticulum was also inhibited by vanadate under the conditions where the turnover rate of $Ca^{++}-ATPase$ was made to increase. These results suggest that the inhibition of $Ca^{++}$ uptake by vanadate may be correlated with that of $Ca^{++}-ATPase$ if experimental conditions are properly set.

• The Korean Journal of Physiology
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• v.10 no.1
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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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• v.8 no.1
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• pp.67-76
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• 1974

The effect of saponin on the sodium plus potassium activated ATPase activity was studied in the rabbit red cell ghosts and the experiments were also designed to determine the mechanism of action of saponin on the APTase activity. The following results were observed. 1. The ATPase activity of rabbit red cell ghosts is inhibited by low concentration of saponin but increased by high concentration. The activating effect of saponin on the $Na^{+}-K^{+}-ATPase$ activity is inhibited by ouabain but the stimulation of the $Mg^{++}-ATPase$ by high concentration of saponin is not inhibited by ouabain. 2. The activity ratio of $Na^{+}-K^{+}-ATPase$ by high concentration of saponin 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 activity ratio of the enzyme by saponin is decreased by raising the calcium concertration 4. The action on the ATPase activity was not related to the amino group of lysine, the hydroxyl group of threonine, the imidazole group of histidine, or the carboxyl group of aspartic acid. 5. The action of saponin on the ATPase activity is due to sulfhydryl group of the enzyme of $Na^{+}-K^{+}-ATPase$.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.2
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• pp.73-78
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• 1992

To investigate the desirable index for evaluation of frozen surimi's grades, the relationship between indices for grading of surimi, such as ATPase activity $(Ca^{2+}-,\;Mg^{2+}-\;and\;EDTA-)4, solubility, viscosity and K-value of frozen surimi and jelly strength of kamaboko was studied. The myofibrillar $Ca^{2+}-ATPase$ activity and solubility from frozen surimi of grades SA, FA, A, RA and B gave values of $1.184\pm0.2,\;0.956\pm0.14,\;0.766\pm/0.07,\;0.453\pm0.07\;and\;0.227\pm0.08$(umoles Pi/min/mg) for $Ca^{2+}-$ATPase activity and $93.19\pm5,\;84.62\pm4,\;70.63\pm5,\;41.21\pm4\;and\;32.82\pm4(\%)$ for solubility, respectively. Therefore, the myofibrillar $Ca^{2+}-$ATPase activity and solubility of surimi were closely related to the jelly strength of kamaboko from same material, as the correlation coefficient were 0.9584 and 0.9849, respectively. K-value, the index of freshness, was related to the jelly strength of frozen surimi as the correlation coefficient 0.9053 and shown as SA $15.67\pm1.4,\;FA\;14.94\pm 3,\;A\;28.00\pm5,\;RA\;32.16\pm3\;and \;B\;48.68\pm 5(\%)$. $Mg^{2+}-$ and EDTA-ATPase activity and viscosity were not related to the jelly strength. The $Ca^{2+}-$ATPase activity and solubility were found to be useful index for evaluating the quality of frozen surimi.

• Journal of Aquaculture
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• v.17 no.3
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• pp.167-172
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• 2004

Chemoenzymatic method was used in this study to evaluate the quality of cultured red seabrim. Level of ATP related compounds, ATPase and Adenylate energy charge (AEC) well reflected changes in condition of fish. ATP level in the muscle of exercised cultured red seabream was decreased significantly during cultured period. In contrast, the level of ADP in the muscle was increased during the period. Level of ATP related compounds in the muscle of cultured red seabream without exercise didn't show significant difference compared to the exercised group. AEC value in muscle of cultured red seabream without exercise was 0.89$\pm$0.02, while AEC value of the exercised group was 0.88$\pm$0.04. ATP and AEC levels among different size of fish did not show any significant difference. AEC value in all sample was higher than 0.8, indicating that the condition of cultured fish was healthy. Activity of Mg2$^{＋}$ (＋Ca2$^{＋}$), Mg2$^{＋}$ (-Ca2$^{＋}$) and Ca2$^{＋}$-ATPase during culture period did not change significantly, regardless of exercise. Therefore, the AEC appears to have some validity as fish health indicator.

• The Korean Journal of Mycology
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• v.19 no.3
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• pp.220-225
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• 1991

Activities of the $F_1-ATPase$ purified from Lentinus edodes were stimulated by $Fe^{3+},\;Fe^{2+},\;Cd^{2+},\;Mg^{2+},\;K^{+}\;and\;Co^{2+}$ but were inhibited by $Zn^{2+},\;Ca^{2+},\;Cu^{2+}\;and\;Ni{2+}$ ion. The enzyme activities were increased 130, 65, 65, 68, 105% and 23% by the 5mM $Fe^{3+}$, 10 mM$Fe^{2+}$, 1mM $Cd^{2+}$, 5mM $Mg^{2+}$, 5mM $K^{+}$ and 5mM$Co^{2+}$ ion addition, respectively, as compared with those not added. The enzyme activities were decreased 18, 19, 27 and 30% by 10 mM $Zn^{2+}$, 10mM $Ca^{2+}$, 0.5 mM $Cu^{2+}$ and 10 mM $Ni^{2+}$ ion, respectively. Anion effects of 10 mM ${Co_3}^{2-}$, 20 mM,$CN^{-}$ 20 mM$CH_3COO^{-}$ and 20 mM ${NO_3}^{-}$ ion were inhibited to the enzyme activities of 98, 95, 70 and 50%, respectively. As increasing of ${SO_4}^{2-}$ ion concentration, the enzyme activity was stimulated and 20 mM ${SO_4}^{2-}$ ion was shown increased of 21%.

• Applied Biological Chemistry
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• v.45 no.2
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• pp.53-58
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• 2002

Quinacrine, a pH-sensitive fluorescence probe, which exists either as an unprotonated fluorescence form or a protonated noufluorescence form, can be used to measure the proton transport activity of $H^+-ATPase$. Quinacrine was used to determine the optimal conditions for measuring the activity of microsomal $H^+-ATPase$ prepared from the roots of tomato plants. The amount of quinacrine fluorescence quenching obtained at $0.43{\mu}g/{\mu}l$ of microsomal protein concentration was 25-26%, which shows that the enzyme activity of 100 nmol/min decreases 10% of quinacrine fluorescence. Maximal fluorescence quenching was obtained at pH 7.0-7.2 and 2 mM $Mg^{2+}$ Because the activity of microsomal $H^+-ATPase$ is also maximal at these conditions, the quinacrine fluorescence well represents the activity of $H^+-ATPase$. Vanadate and $NO_3-$, specific inhibitors of plasma and vacuolar $H^+-ATPases$, respectively, were successfully applied to inhibit the quinacrine fluorescence quenching mediated by the corresponding $H^+-ATPases$. These results imply that quinacrine is a useful tool for measuring the proton transport activities of microsomes obtained from the root tissue of tomato plants.

• Advances in Traditional Medicine
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• v.5 no.2
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• pp.137-143
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• 2005

Doxorubicin induces oxidative stress leading to cardiotoxicity causing electrocardiogram abnormalities and increases in biomarkers associated with toxicity. Green tea extract (GTE) is reported to possess antioxidant activity mainly via its polyphenolic constituent, catechins. This study was intended to determine the effect of various doses of GTE (25, 50 and 100 mg/kg/day p.o. for 30 days) on doxorubicin-induced electrocardiographic and biochemical changes in rat heart. The latter included lactate dehydrogenase, creatine kinase, and glutamic oxaloacetate transaminase in serum and superoxide dismutase, catalase, and reduced glutathione, as well as membrane bound enzymes like $Na^+K^+ATPase,\;Ca^{2+}ATPase,\;Mg^{2+}ATPase$ and decreased lipid peroxidation in heart tissue Results demonstrated that rats which received GTE were less susceptible to such changes indicating protection afforded by GTE.