• 한국동물학회지
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• 제15권4호
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• pp.163-182
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• 1972

토끼의 골격근 小胞體의 ATPase 活性과 Ca吸收能에 미치는 caffeine의 영향을 조사 하였다. 遠心分離로 分劃된 小胞體에서 $2,000 \\sim 8,000 \\times G$ 分劃의 ATPase 活性은 caffeine에 의하여 增大되지만 $8,000 \\times G$ 以上의 分劃에서는 아무 영향도 받지 않았다. Caffeine에 의한 이 活性增大는 이 分劃에 混在하는 mitochondria의 ATPase 活性이 增大 된 結果라고 해석된다. 小胞體의 $2,000 \\sim 10,000 \\times G$ 分劃과 $10,000 \\sim 20,000 \\times G$ 分劃의 Ca吸收能도은 反應液內 Ca의 농도가 200 nmoles/mg protein 정도 이상일 때는 caffeine에 의하여 현저히 阻害되지만, Ca의 농도가 이 以上이 때는 2,000$\\sim$10,000 分劃에서만 이 阻害現象을 볼 수 있다. 低農度 Ca에서의 이 阻害現象은 caffeine에 의하여 mitochondira의 Ca吸收도 阻害되기 때문에 나타나는 것으로 해석된다. Caffiene에 의한 筋收縮의 誘發 및 逕縮現象은 筋小胞體의 Ca 吸收가 이 特質에 의하여 阻害되고 또 蓄積된 Ca이 放出되기 때문에 일어나는 것으로 해석된다.

• 한국식품영양과학회지
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• 제14권1호
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• pp.77-81
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• 1985

사양기간(飼養期間)이 서로 다른 닭의 골격근에서 actomyosin 을 추출하여 추출성과 생물 활성을 비교하였다. 가슴부위에서 추출한 actomyosin의 추출성은 사양기간(飼養期間)이 3,4,5,6,7주(週)의 순으로 각각 184.5, 364.0, 784.8, 926.1, 985.2, 1020.1 mg/100g 이었고 다리부위는 각각 28.6, 70.8, 137.9, 139.5, 608.3 그리고 646.2mg/100g 이었다. 사양기간(飼養期間)이 3,6,8주(週)인 경우 24시간 추출한 actomyosin의 EDTA-ATPpase활성은 각각 0.68, 0.59, 0.50${\mu}M$ Pi/mg protein min. 이었고 Mg^{+2}$-ATPase 활성은 각각 0.66, 0.71, 0.75 $0.50\;{\mu}M$ Pi/mg protein min.이었고 Mg^{+2}$-ATPase 활성은 각각 0.66, 0.71, $0.75\;{\mu}moles$ Pi-mg protein/min.이었다. 사양기간(飼養期間)에 관계없이 actomyosin 의 3, 6, 8 Mg^{+2}$-ATPase 활성은 저(低) ion 강도에서 높은 활성과 rh(高) ion 강도에서 낮은 biphasic response를 나타내었고 $125\;{\mu}mole$ EGTA로서 Mg^{+2}$-ATPase 활성을 $0.1\;{\mu}mole/mg$ protein/min 이하로 저해시켰다.

• Fisheries and Aquatic Sciences
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• 제8권1호
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• pp.10-16
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• 2005

Conditions for sufficient and rapid distribution of a cryoprotectant (sorbitol solution) into intact fish muscle (Oncorhynchus mykiss) were studied as changing in the residual Ca2+ ATPase activity during freeze/thaw cycling. Chunks of the fish muscle were immersed in 4 concentrations of sorbitol solutions ($20\%$, $30\%$, $45\%$, and $60\%$) by a shaker mechanism at 5$^${circ}C. Whole immersion samples (W) showed a higher value of the residual Ca2+ ATPase activity than those in the untreated controls (C), except in the treated controls (TC), while less effect of immersion concentration could be found. Comparing the extent of penetration of sorbitol into the surface layer to inner layer of immersed fish chunks, outer portion samples achieved excellent cryoprotection with $100\%$ of the residual ATPase activity values or more. For the inner portion samples, $30\%$ and $45\%$ sorbitol solution treatments indicated a higher ATPase activity than $60\%$ treatment. At high concentrations, mass transfer rates during osmotic dehydration might berapid and it causes faster surface drying by dewatering at surface solute layer. Periodically immersed and relaxed samples, W (5-3-1), led to good cryoprotection effect: W (5-3-1) indicated high residual Ca2+ ATPase activity values and the residual ATPase activity values excess $100\%$ in immersion of $30\%$ and $45\%$ sorbitol solutions.

• Journal of Microbiology and Biotechnology
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• 제9권4호
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• pp.414-421
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• 1999

Helicobacter pylori were found to be resistant to azide but sensitive to vanadate, suggesting that defect in the P-type ATPase activity rather than F-type ATPase would be lethal to cell survival or growth. To elucidate the relationship between this enzyme inhibition and H. pylori death, we determined the effect of omeprazole (OMP) plus vanadate on enzyme activity and cell growth. The minimum inhibitory concentration (MIC; ca. 0.8$\mu$mol/disk) of vanadate for H. pylori growth was lowered over l0-fold with the aid of OMP, whereby its inhibitory potential toward the P-type ATPase activity was diametrically increased. Alternatively, we found that this enzyme activity was essential for active transport in H. pylori. From these observations, we strongly suggest that the immediate cause of the growth inhibition of H. pylori cells with OMP and/or vanadate might be defective in the cell's active transport due to the lack of P-type ATPase activity. From the spectral data with circular dichroism (CD) spectroscopy, we found that activated OMP (OAS) at concentration below MIC did not disrupt helical structures of membrane proteins. Separately, we determined the cytopathic effect of OAS by SDS-PAGE, indicating the change in the production of cytoplasmic protein but not cell membrane.

• Biotechnology and Bioprocess Engineering:BBE
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• 제8권3호
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• pp.192-198
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• 2003

BiP, immunoglobulin binding protein, is an ER homologue of Hsp70. However, unlit other Hsp70 proteins, regulatory protein(s) for BiP has not been identified. Here, we demo strafed the presence of potential regulatory proteins for BiP using a pull -down assay. Since BiP can bind any unfolded protein, only the ATPase domain of BiP was used for the pull -down assay in order to minimize nonspecific binding. The ATPase domain was cloned to produce recombinant protein, which was then conjugated to CNBr-activated agarose. The structural conformation and ATP hydrolysis activity of the recombinant ATPase domain were similar to those of the native protein, light proteins from metabolically labeled mouse plasmacytoma cells specifically bound to the recombinant ATPase protein. The binding of these proteins was inhibited by excess amounts of free ATPase protein, and was dependent on the presence of ATP. These proteins were eluted by ADP. Of these proteins, Grp170 and BiP where identified. while the other were not identified as known ER proteins, from Western blot analyses. The presence of the ATPase-binding proteins for BiP was first demonstrated in this study, and our data suggest similar regulatory machinery for BiP may exist in the ER, as found in prokaryotes and other cellular compartments.

• 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.

• 한국식품영양과학회지
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• 제18권1호
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• pp.123-130
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• 1989

방어로부터 추출한 근원섬유 현탁액을 $0^{\circ}C$(빙장), $-3.5^{\circ}C$(PF저장), $-20^{\circ}C$(동결저장)에 저장하면서 Ca-과 Mg-ATPase활성을 측정하여 근육단백질의 변성을 조사하였으며 일부는 생선을 각 온도에 일정기간 저장한 후 근원섬유를 추출하여 단백질 변성정도를 비교한 결과 추출한 근원섬유를 저장하였을 때 빙장 및 PF저장한 시료의 ATPase활성은 비슷한 수준이었으나 동결 저장한 시료에서는 현저히 낮았다. 생선을 각 온도에 1주일간 저장한 후 추출한 근원섬유의 소활성은 근원섬유를 미리 추출하여 같은 기간동안 저장한 경우에 비하여 빙장과 PF저장에서는 1.2-1.8배, 동결저장에서는 2.5-3배 정도 높은 수준을 유지하고 있었다. 근원섬유를 각 온도에 저장하였을 때의 변성속도는 Ca-의 경우가 Mg-ATPase에 비 해 2-3배 빨랐으나 생선으로 저장한 경우에는 Ca-과 Mg-ATPase간에 큰 차이를 나타내지 않았다.

• The Korean Journal of Physiology
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• 제8권1호
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• pp.55-65
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• 1974

The effect of ginseng on the ATPase activity of rabbit ref cell membrane has been investigated. The experiments were also designed to determine whether the components of ginseng could be attributed to the effect on ATPase activity which dependent upon sodium plus potassium and is sensitive to ouabain. The following results were observed. 1. The activity of the $Na^{+}-K^{+}-ATPase$ from red cell membrane is stimulated by ginseng, and the concentration of ginseng for half-maximal activity is about 15 mg%. The pH optimum for the ginseng sensitive component is 7.6. 2. The portion of the enzyme activity stimulated by ginseng is completely abolished by ouabain. 3. The activating effect of ginseng on the ATPase, with a given concentration of sodium in the medium, is increased by raising the potassium concentration but activity ratio is decreased. 4. The activating effect of ginseng on the ATPase, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but the activity ratio is decreased. 5. The ATPase activity is increased by small amounts of calcium but inhibited by larger amounts and the rate of activity by ginseng is constant. 6. The action of ginseng on the ATPase activity was not related to the sulfhydryl group of cysteine, the amino group of lysine, the imidazole group of histidine, the quanidinium group of arginine, the carboxyl group of aspartic acid, or the hydroxyl group of threonine. 7. The activating effect of ginseng on the ATPase activity may be not due to a saponin which is contained in ginseng.

• 대한약리학회지
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• 제8권1호
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• pp.31-40
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• 1972

The author studied the actions of ouabain and diphenylhydantoin sodium on the ATPase activity in mitochondrial fraction isolated from rabbit heart and compared with that of quinidine. The results obtained are as follows: 1) In studying the $(Na^++K^+)-activated$ ATPase activity, the rabbit heart isolated was immediately frozen for 7-9 days (ageing of preparation) and thereafter the mitochondria1 fraction obtained by differential centrifugation technic was treated with solution A containing 0.15% deoxycholate for 24-48 hours at $-10^{\circ}C$ before using in experiment. These methods increased the activity ratio to 0.87-0.98. 2) The $(Na^++K^+)-activated$ ATPase activity in mitochondrial fraction of rabbit heart was not completely but markedly inhibited by ouabain. This inhibitory action of ouabain was moderately antagonised by $K^+$ concentration at constant Na concentration. 3) Diphenylhydantoin sodium in concentration of $5{\times}10^{-4}{\sim}10^{-3}M$ stimulated markedly not only $Mg^{++}-dependent$ ATPase activity but also $(Na^++K^+)$-activated ATPase activity and in concentration lower than $10^{-6}M$ had little effect. However, this effect of diphenylhydantoin was markedly increased in the presence of $Na^+$ alone rather than $K^+$ alone, but lesser than that effect in the presence of both $Na^+$ and $K^+$, together. The stimulating effect of diphenylhydantoin was specifically antagonized by ouabaion. 4) When the rabbits were intravenously injected with ouabain and diphenylhydantion respectively, $(Na^++K^+)-activated$ ATPase activity of rabbit heart of ouabain-treated group was much decreased and both $(Na^++K^+)-activated$ ATPase and $Mg^{++}-activated$ ATPase activity were moderately increased in diphenylhydantoin-treated rabbit group. 5) The $(Na^++K^+)-activated$ ATPase activity in mitochondrial fraction of rabbit heart was slightly inhibited by quinidine in high concentration of $10^{-4}M$, but nearly little effect was observed below the concentration of $5{\times}10^{-5}M$. 6) It might be possible to conclude that diphenylhydantoin specifically antagonised the action of ouabain on the membrane ATPase, which is different from the action of quinidine.

• 약학회지
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• 제41권3호
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• pp.345-351
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• 1997

The purpose of this investigation was to determine the inhibition of $Na^+,\;K^+$-ATPase, cyclicAMP phophodiesterase and platelet activation by secondary metabolites isolated from mar ine organisms. The secondary metabolites were isolated and identified as six diterpenoids(1 : astrogorgin, 2 : ophirin, 3 : calicophirin B, 4, 5 and 6 : cladiellin) from the dichloromethane extract of Muricellajsp., four ceramides(1,2,3, and 4) from Acabaria undulata and three antharaquinones(1,2 : crysophanol, and 3 : physcion) from Urechis unicintus. The results demonstrated that diterpenoids(2,3, and 4) showed the inhibition of cyclicAMP phosphodiesterase, and ceramides(1,3, and 4) showed the inhibition of cyclicAMP phosphodiesterase and thrombin(0.1 units/ml)-induced aggregation of washed rabbit platelet, and anthrapuinones((1,2, and 3) showed the inhibition of $Na^+,\;K^+$-ATPase. Among the anthraquionones, 1,2-dimethoxy-3-methyl-8-hydroxy-anthraquinone(1) showed the inhibition of collagen(1.0 ${\mu}g$/ml)-induced aggregation in a concenration-dependent manner with IC50 value of 42.8 ${\mu}g$M.