• Journal of Nutrition and Health
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• v.11 no.3
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• pp.37-42
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• 1978

Actomyosin and myofibril were extracted from Korean native Goat muscle with the Weber-Edsall solution. ATPase activities and physiochemical properties were measured. The results obtained were as follows; 1) Mg-activitied ATPase activity of actomyosin and myofibrill from Korean native Goat muscle exhibited a common biphasic response, a typical ATPase pattern, that is high at a low ionic strength and low at a high ionic strength. Actomyosin showed high activity than myofibrill. 2) Mg-activited ATPase activity of actomyosin from muscle increased extraction time 24 hours. 3) EDTA-enhanced ATPase activity of actomyosin was greater than myofibrill and low at the low ionic strength, high at the high ionic strength. The difference of the activity were shown great broad pattern at the after 0.3M KCI concentration. 4) Effect of EGTA on-ATPase activity of myofibrill and actomyosin from muscle was measured, the Mg-ATPase activity was markedly depressed. 5) Solubility of actomyosin from muscle began to solubilize at KCI concentration of 0.28M and solubilized completely at the KCI concentration of 0.3M.

• Journal of Korean Society on Water Environment
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• v.18 no.4
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• pp.395-400
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• 2002

Lead is one of the most toxic metal and is detectable in practically all phases of environment and in all biological system. Transport, industrial and domestic waste products are the main sources of this pollutant. Ingested lead is rapidly absorbed and widely distributed throughout the body, causing extensive tissue damage. In this study, we chose the freshwater decapods Maceobrachium nipponnese as a sensitive indicator organism for environmental pollution. In order to investigate the possibility in use of $Na^+/K^+ATPase$ activity as a biomarker of lead pollution, we tested the acute toxicity of lead to Maceobrachium nipponnese. The $LC_{50}(96hr)$ value for lead in Maceobrachium nipponnese was found to be $446{\mu}g/L$ with the 95% confidence limits. The lead exposure group at $LC_{50}$ showed a significant $Na^+/K^+ATPase$ inhibition, depending on the exposure time. Comparision of several concentrations of lead revealed that the $Na^+/K^+ATPase$ activity in Maceobrachium nipponnese was significantly decreased in a concentration dependent manner. These results suggest that $Na^+/K^+ATPase$ activity in Maceobrachium nipponnese may possibly be used as a biomarker of lead pollution in aquatic ecosystem.

• The Korean Journal of Zoology
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• v.14 no.2
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• pp.43-56
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• 1971

The Ca uptake by the fragmented sarcoplasmic reticulum of the rabbit skeletal muscle was measured under various concentrations of K, Mg, Caffeine, procaine and quinine. The ATPase activity of this reticular membrane was measured under the same conditions simultaneously. The saturation of Ca uptake was almost completed within 1 minute. The Ca uptake was inhibited by high concentrations of K (above 50 mM) and Mg (above 1 mM)in the absence of ATP. When ATP is present, however, the Ca uptake did not reflect the concentration of K, while it increased greatly as the concentration of Mg was increased. Caffeine and procaine caused the inhibition of Ca uptake in the presence of ATP, but quinine did not. The ATPase activity of the membrane was little affected by the concentration of K, while it was enhanced in the presence of Mg. Caffeine, procaine and quinine did not influence the ATPase activity.

• Korean Journal of Veterinary Research
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• v.23 no.1
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• pp.9-16
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• 1983

The effects of ethanol on Na-K-ATPase activity were investigated with cat kidney homogenate. The results were summarized as follows: 1. Na-K-ATPase activity was inhibited with dose-dependent manner by ethanol of higher concentration than 1%, and showed an estimated $I_{50}$ (the inhibitor concentration to cause 50% inhibition) of 7.5%. 2. Hydrolysis of ATP was linear with the incubation time in the absence and presence of 8% ethanol, whereas it was different with preincubation time in the presence of 15% ethanol. 3. Inhibition of Na-K-ATPase activity by ethanol was not affected by increased enzyme concentration, and showed the reversibility of the inhibitory pattern. 4. Kinetic studies of cationic-substrate activation of Na-K-ATPase showed that ethanol had both properties of classical competitive inhibition for $Mg^{{+}{+}}$ or $K^+ and non-competitive inhibition for ATP or $Na^+$. 5. Arrhenius plot yield two break point at $21^{\circ}$ and $30^{\circ}C$ in the absence of ethanol, whereas showing only one break point at $18^{\circ}C$ in the presence of 8% ethanol. These results suggested that ethanol inhibited Na-K-ATPase activity reversible through a disturbance of microenvironment of lipids associated with the enzyme.

• YAKHAK HOEJI
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• v.29 no.2
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• pp.76-89
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• 1985

The effects of ginseng saponin on the activity, phosphorylation, [$^{3}$H] ouabain binding and light scattering (disruption) of purified $Na^{+}$ ,$K^{+}$ -ATPase isolated from the outer medulla of sheep kidney were compared to those of gypsophila saponin, sodium dodecylsulfate (SDS), and Triton X-100 on the same parameters. $Na^{+}$ , $K^{+}$ -ATPase activity, phosphorylation, and [$^{3}H$] ouabain binding were inhibited by ginseng saponin (triol>total>diol), SDS, or Triton X-100, but increased by gypsophila saponin. Low doses of ginseng saponin (3.mu.g saponin/.mu.g protein) decreased phosphorylation sites and ouabain binding site concentration (Bmax) without any change of turnover number and affinity for ouabain binding which were decreased by high dose of ginseng saponin (over 10.mu.g saponin/.mu.g protein), SDS or Triton X-100. On the other hand, gypsophila saponin increased the affinity without any change of Bmax for ouabain binding. Inhibition of $Na^{+}$ ,$K^{+}$ -ATPase activity by ginseng saponin and SDS or Triton X-100 appeared before and after decrease in light scattering, respectively. These data suggest that ginseng saponins (total, diol, triol saponin) inhibit $Na^{+}$ , $K^{+}$ -ATPase activity by specific direct and general detergent action at low and high concentrations, respectively, and this inhibitory action of ginseng sapornin to $Na^{+}$ , $K^{+}$ -ATPase is not general action of all saponins.

• The Korean Journal of Nuclear Medicine
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• v.32 no.2
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• pp.121-128
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• 1998

Purpose: $Na^+-K^+$ ATPase activity has been estimated by the degree of inhibition of cation transport by cardiac glycosides (ouabain) using Rb-86 as a substrate. The biological characteristisc of T1-201 is known to be similar to those of potassium as a transport substrate in the presence of glucose, insulin or phobol myristate acetate (PMA). The purpose of this study was to measure ouabain sensitive $Na^+-K^+$ ATPase activity using T1-201 and compare with that using Rb-86. Materials and Methods: Smooth muscle cells isolated from rat aorta or human placental umbilical artery were cultured, and used to measure cellular $Na^+-K^+$ ATPase activity. $Na^+-K^+$ ATPase activity was measured as a percentage decrease in cellular uptake of T1-201 or Rb-86 by ouabain under the presence of glucose, insulin or PMA in media. Results: $Na^+-K^+$ ATPase activity measured with T1-201, as a transport substrate, was not different from those measured with Rb-86 in rat or human smooth muscle cell preparation. Incubation with high concentration glucose resulted in about 30% decrease in enzyme activity. In contrast, insulin or PMA resulted in 10-70% or 28% increases from baseline activity, respectively. Conclusion: These results suggests that 71-201 could replace Rb-86 in measurement of ouabain sensitive $Na^+-K^+$ ATPase activity in vitro. High level of glucose concentration decreased cellular $Na^+-K^+$ ATPase activity, but insulin or PMA increased it.

• Journal of Life Science
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• v.21 no.5
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• pp.671-677
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• 2011

We previously reported the isolation and characterization of a gene, SCA1 (for soybean $Ca^{2+}$-ATPase 1), encoding a calmodulin-regulated $Ca^{2+}$-ATPase that is located in the plasma membrane in soybean. Here, a $Ca^{2+}$-ATPase designated as SCA2 was isolated from soybean. The two $Ca^{2+}$-ATPases, SCA1 and SCA2, share a remarkably high degree of similarity (78%). Ten transmemebrane domains were predicted by hydropathy analysis. Using gel overlay assays, CaM was found to bind to SCA2 in a $Ca^{2+}$-dependent manner. Southern blot analysis revealed the presence of two copies of the $Ca^{2+}$-ATPase gene in the soybean genome. An N-terminal truncation mutant that deletes sequence through the putative calmodulin binding site was able to complement a yeast mutant (K616) that was deficient in two endogenous $Ca^{2+}$ pumps. Our results indicate that SCA2 is structurally highly conserved with type IIB $Ca^{2+}$ pumps in plants.

• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.1
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• pp.123-130
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• 1989

Myofibrillar protein(myofibil) was prepared from Yellowtail fish (Seriola quinqueradiata), and then, it was stored at $0^{\circ}C$(ice-cooling), $-3.5^{\circ}C$(partial freezing) and $-20^{\circ}C$(freezing). Another myofibrils were prepared from the fish stored with ice-cooling, partial freezing and freezing for a week as the maximum. Denaturation of muscle protein during the storage was investigated by the measurement of $Ca^{2+}-$ and $Mg^{2+}-ATPase$ activity. Specific activity of $Ca^{2+}-\;and\;Mg^{2+}-ATPase$ associated with Yellowtail myofibrils was 0.155 and $0.149\;{\mu}\;mole$ Pi/min/mg of protein, respectively, before storgae. ATPase activity of myofibils did not show any significant difference between $0^{\circ}C$ and $-3.5^{\circ}C$ whereas it was decreased faster at $-20^{\circ}C$ than at $0^{\circ}C$ or $-3.5^{\circ}C$. ATPase activity of myofibirls extracted from the fish stored for a week was 1.2-1.8 times higher than myofibils stored with ice-cooling or partial freezing while it was 2.5-3 times higher than that with freezing. Apparent denaturation constant of $Ca^{2+}-ATPase$ of myofibrils was between 0.48-0.65, and it was 2-3 times higher than that of $Mg^{2+}-ATPase$. The constant of myofibrils extracted from the fish did not show significant difference between $Ca^{2+}-\;and\;Mg^{2+}-ATPase$.

• Proceedings of the Korean Biophysical Society Conference
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• 2002.06b
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• pp.9-11
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• 2002

Plasma membrane Na$^{＋}$-K$^{＋}$ ATPase (pump) is an essential component to maintain asymmetrical ion distribution across cell membrane. The Na$^{＋}$-K$^{＋}$ ATPase was discovered by Jens C. Skou in 1957 and since then physiological and biochemical properties of the enzyme have been extensively studied. Jens C. Skou was awarded the 1997 Nobel Prize in chemistry for his discovery of the Na $^{＋}$ - $K^{＋}$ ATPase.(omitted)

• Korean Journal of Fisheries and Aquatic Sciences
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• v.31 no.4
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• pp.545-552
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• 1998

This study was undertaken to clarify the effects of electrical stimulation on the biochemical properties of plaice sarcoplasmic reticulum and myofibrils at early period of death. The plaices were electrically stimulated (110V/60 Hz) In sea water bath for 15, 35, and 60 seconds, and killed instantly by spiking at the head. Killed samples were investigated for the changes in $Ca^{2+}$-ATPase activity of FSR (fragmented sarcoplasmic reticulum), LSR (light SR), HSR (heavy SR), and SDS-PAGE pattern of FSR. $Ca^{2+}$-ATPase activity of FSR increased until $45^{\circ}C$ and inactivated over $50^{\circ}C$. $Ca^{2+}$-ATPase activity of FSR remarkably decreased according to the duration of electrical stimulation. Myofibrillar $Mg^{2+}$-ATPase activity of electrically stimulated plaices in the presence of $Ca^{2+}$ was higher than that of sample instantly killed by spiking. $Mg^{2+}$-ATPase activity of myofibrils increased by electrical stimulation and the activity decreased during storage at $5^{\circ}C$. Myofibrillar $Mg^{2+}$-ATPase activity in sample killed by spiking was not affected by $Ca^{2+}$ ion. Myofibrillar $Mg^{2+}$-ATPase activity of electrically stimulated sample in the absen-re of $Ca^{2+}$ decreased during storage at $5^{\circ}C$, whit $Mg^{2+}$-ATPase activity in unstimulated sample did not show any change. $Ca^{2+}$-sensitivity of myofibrils showed no differences between electrically stimulated sample and sample killed by spiking, and the was no change during at $5^{\circ}C$.