• 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.

• 환경위생공학
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• 제13권1호
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• pp.157-165
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• 1998

The purpose of this study is to explain the relations between pine needle tyrosinase's activity and quantity of minerals in the Waters' mineral water. Pine needle tyrosinase's activity was measured by metal ions' concentration like Ca, Mg, Na, K, and Fe in different kinds of drinking water. 1. Pine needle tyrosinase has the highest activity when Ca's concentration is 14.40mg/L while the activity decreases by 92% when it is 108.10 mg/L. Therefore, the resonable range of Ca concentration for drinking water is 10-100.0 mg/L. 2. Mg has higher Pine needle tyrosinase's activity than Ca by three times. The reasonable range of Mg concentration for drinking water is 3.0-10.0 mg/L. 3. Pine needle tyrosinase has the highest activity when Na's concentration is 15.70 mg/L. The reasonable range of Na concentration for drinking water is less than 15 mg/L. 4. The activity increases as K concentration rises. In normal kinds of drinking water, K concentration is less than 10 mg/L. Since K has impacts on the activity only when its concentration is more than 10 mg/L, no problem in expected. 5. Fe has some impacts on the activity when its concentration is more than 10mg/L. As most kinds of drinking water contain less than 0.3 mg/L, no problem is expected. With above-mentioned observations, it is concluded that Water's mineral water contains reasonable levels of minerals like Ca, Mg, K and Na.

• The Korean Journal of Physiology
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• 제8권1호
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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 $Na^{+}-K^{+}-ATPase$.

• Journal of Plant Biology
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• 제29권4호
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• pp.285-294
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• 1986

The present study was attempted to investigate the effects of polyamines such as putrescine, spermidine and spermine on protein content and DNase activity in vivo and in vitro in carrot embryos. It was also investigated whether polyamines could replace role of cations required for DNase activity in vitro. The results obtained are as follows. Putrescine, spermidine and spermine increased protein content, although response to spermine reached plateau at the concentration of 0.1 mM. DNase activity was inhibited by polyamines, the inhibition being concentration-dependent and the highest att he concentration of 10 mM. The inhibition of DNase activity was the most prominent with spermine. Similar inhibitory effect to polyamines which was concentration-dependent was found in DNase activity but no change was shown on time-course in vitro. Putrescine and spermidine enhanced the DNase activity at low Mg2+ and Mn2+ concentrations, suggesting that the role of Mg2+ and Mn2+ for DNase activity could be, in part, replaced by these polyamines. These results, therefore, suggest that plyamines can modulate DNase activity through binding to DNA rather than direct effect on DNase activity.

• 대한한의학방제학회지
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• 제9권1호
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• pp.335-354
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• 2001

This study was designed to investigate biological activity of antler extract added medical plants. The scavenging activity of DPPH radical was low scavenging activity at 0.01% concentration. But in the 0.05% and higher concentration, electron donating ability(EDA) is above 50% except Kongindangagam(48.5%) and significantly good above 70% in the 4 extracts. Superoxide dismutase(SOD)-like activity was 44.3% and 45.1% extracts of Ohjayenjongwhangami and M(market sample), Inhibition of xanthine oxidase were above 50% at 0.5% concentration except Boshingiwhangwhangami and from 62.4% to 84.9% in the 4 extracts. Inhibition rate of boshingiwhangwhangami was hasty increased from 33.5% to 77.5% at 1.0% concentration and others the higher concentration, the more increasing inhibition. Angiotension I-converting enzyme(ACE) inhibitory activities were high activity all of extracts. In the 0.5% concentration, ACE inhibition was above 80%. Especially 0.01% concentration of M was presented 81.8%. The study which conducted to investigate the effect of feeding antler extract group for 50 days on sperm concentration, Ca contents of serum, kidney and femur in rats was higher than that saline group.

• 한국환경과학회지
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• 제13권4호
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• pp.413-420
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• 2004

The objectives of present study were to investigate the effects of benzo[a]pyrene(BaP) on cytotoxicity, lipid peroxidation and antioxidant enzymes in rat hepatocyte primary culture. Primary cultures of rat hepatocytes were incubated for 24 hr, 48 hr or 72 hr in the presence of various concentrations (0, 10, 20, 30, 50 or 100 $\mu.$ M) of BaP. Cytotoxicity and cell viability were determined by measuring glutamic oxaloacetic transaminase(GOT) activity, lactate dehydrogenase(LDH) activity and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide(MIT) value. Lipid peroxidation was evaluated using thiobarbituric acid reactive substances(TBARS) assay. Effects on antioxidant system were determined by measuring glutathione peroxidase(GPx) activity, glutathione reductase(GR) activity and glutathione concentration. Activities of GOT and LDH, MTT value as well as TBARS concentration were not affected by up to 100 $\muM$ of BaP for 24 hr incubation. However, BaP at the concentration of 50 $\muM$ for 48 hr incubation or at the concentration of 30 $\muM$ for 72 hr incubation began to increase LDH activity and TBARS concentration but decrease MTT value, representing that BaP caused cytotoxicity and decreased cell viability in dose- and time-dependent manners. GPx activity began to be decreased by BaP at the concentration of 50 $\muM$ for 72 hr incubation. Whereas, GR activity began to be decreased by BaP at the concentration of 20 $\muM$ for 72 hr incubation. Glutathione concentration began to be decreased by BaP at the concentration of 20 $\muM$ for 72 hr incubation and was further reduced to 90% by 100 $\muM$ of BaP. These results demonstrate that BaP caused cytoctoxicity and decreased cell viability by increasing lipid peroxidation and decreasing glutathione concentration as well as activities of GPx and GR.

• 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.

• 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.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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• 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