• Clinical and Experimental Reproductive Medicine
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• v.18 no.2
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• pp.123-131
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• 1991

In order to study the growth and maturation of ovarian follicle, the localization and activity of alkaline phosphatase(ALPase) and adenosine triphosphatase(ATPase) of the granulosa cells and theca layer were examined according to the follicle size, the follicle state and the ovarian cyclic phase in pig. Theca interna of the small follicles was more heavyly localized with reaction product by the activites of ALPase and ATPase than that of the large follicles. It is assumed that, as the follicles proceed to growth and maturation, antrum formation is the result of the follicular fluid accumulation by means of active transport by the activities of ALPase and ATPase in theca interna. The activities of ALPase and ATPase in atretic follicles were higher than those of normal follicles. These results imply that the mechanisms of follicle maturation and atresia are different according to the phase of ovarian cycle.

• The Korean Journal of Mycology
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• v.19 no.3
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• pp.214-219
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• 1991

Adenosine-5'-triphosphatase$(F_1-ATPase)$ in the Lentinus edodes was fractionated by ammonium aulfate 30% saturation and purified by Sephadex G-200 gel filtration in three times. Three kinds of protein fractions of $F_1-ATPase$ were isolated from this mushroom, and fraction I and ll showed its activity for the substrate, adenosine-5'-triphosphate. Its optimum pH and temperature were found to be pH 7.6 and $58^{\circ}C$, and its thermal stability was stabled for 30 min. at $20-30^{\circ}C$. The Km value of this enzyme was 1.81 mM.

• Horticulture, Environment, and Biotechnology : HEB
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• v.59 no.6
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• pp.835-845
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• 2018

We studied the role of ethylene control in regulating energy metabolism, antioxidant enzyme activity, and vase life of cut rose Rosa hybrida 'Carola'. Rose flowers at stage II were sprayed with one of the following solutions: water (control), $10{\mu}L\;L^{-1}$ 1-methylcyclopropene (1-MCP), or $0.5g\;L^{-1}$ 2-chloroethanephosphonic acid (ethephon). After harvest, ethylene production rate, respiration intensity, energy charge (EC), activities of energy metabolism-related and antioxidant enzymes, and malondialdehyde (MDA) content were measured. Results showed that 1-MCP enhanced the activities of superoxide dismutase, $H^+$-adenosine triphosphatase, $Ca^{2+}$-adenosine triphosphatase, succinic dehydrogenase, and cytochrome c oxidase, increased adenosine triphosphate (ATP) content, maintained high EC levels, inhibited respiration intensity, reduced peroxidase (POD) and polyphenol oxidase (PPO) activity and MDA accumulation, and prolonged vase life. Ethephon promoted ethylene production and respiration intensity, increased POD and PPO activity, reduced ATP content and EC levels, and accelerated senescence. Our results support a novel role for ethylene control in regulating senescence of 'Carola'.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.4
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• pp.349-355
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• 1990

Actomyosine prepared from Yellowtail fish(seriola quinqueradiata) were stored at $0^{\circ}C$(ice-cooling) -3.5$^{\circ}C$(partial freeaing) and -2$0^{\circ}C$(freezing) Another actomyosin samples were prepared from the fish previously stored at the temperatures for a week as the maximum .Remaining activity of {{{{ {Ca }^{2+ } }}}}-and {{{{ {Mg }^{2+ } }}}}- dependent adenosine triphosphatase(ATPase) activity was measured fronm the actomyosin preparations. Specific activity of {{{{ {Mg }^{2+ } }}}}-ATPase of actomy-osin before storagew was 0.253$\mu$ mole pi/min/mg of protein and it was 1.5 times higher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. The enzyme activities were markedly decreased during early period of storage. However no significant differences in the enzyme activity were revealed among the samples stored at different temperature. The enzyme of actomyosin prepared from the fish previously stored at the temperatures for a week revealed an acitivity of 2-3 times higher than that of freezing. Apparent denaturation constant of {{{{ {Mg }^{2+ } }}}} -ATPase of actomyosin was between 0.810-1.139 per day and it was about 1.5 times hgiher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. But the constant of {{{{ {Mg }^{2+ } }}}} ATPase of actomyosin extracted from the fist stored for a week at each temperature was between 0.176-0.356 per day. This constant was 4 times higher than that of {{{{ {Ca }^{2+ } }}}}- ATPase in frozen stored fish. It was presumed from these results that denaturation of ATPase is largely accorded to the structural changes of actomyosin.

• Korean Journal of Pharmacognosy
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• v.16 no.2
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• pp.81-92
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• 1985

The Polygoni Radix and Cynanchi Radix have been used to potentiate the liver functions in clinic of Oriental Medicine. The water extracts of Polygoni Radix and Cynanchi Radix were administered orally to rats intoxicated with carbon tetrachloride and then this experiment have been performed by observing liver fatty degeneration and activities of enzymes such as cytochrome oxidase (CYO), adenosine triphosphatase (ATP), acid phosphatase (ACP), lactate dehydrogenase (LDH) and alkaline phosphatase (ALP). By oral administration of water extracts of the radices between 1 and 10 days, the following results were obtained. 1. The group given Cynanchi Radix extract showed recovery of the fat liver in 4 days, whereas that given Polygoni Radix extract did the recovery in 8 days. 2. In cytochrome oxidase activity, the group given Cynanchi extract showed normal activity in 6 days, whereas that given Polygoni Radix extract did the activity in 8 days. 3. In adenosine triphosphatase activity, the groups given Cynanchi Radix and Polygoni Radix extracts showed normal activities in 2 and 8 days, respectively. 4. In acid phosphatase activity, the groups given Cynanchi Radix and Polygoni Radix extracts showed recovery of the activities in 2 and 4 days, respectively. 5. In lactate dehydrogenase activity, the group given Cynanchi Radix and Polygoni Radix extracts showed recovery of the activities in 6 and 10 days, respectively. 6. In alkaline phosphatase activity, the group given Cynanchi Radix extract showed normal activity in 2 days, whereas that given Polygoni Radix extract showed slight recovery between 4 and 6 days followed by decrease of the activity in 8 and 10 days. From the above-mentioned results, it was found that both of the water extracts of Polygoni and Cynanchi Radix possessed the recovery action of liver function as intoxicated with carbon tetrachloride in rats. It is also noted that the extract of Cynanchi Radix showed more potent activity than that of Polygoni Radix.

• Journal of Radiation Protection and Research
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• v.14 no.1
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• pp.1-7
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• 1989

In order to evalulate the cause of polyuric acute tubular necrosis, we measured electrolytes, $Na^{+}\;and\;K^{+}$ excreted in urine, and activities of $Na^{+}-K^{+}$adenosine triphosphatase ($Na^{+}-K^{+}$ATPase) Excretion of $Na^{+}\;and\;K^{+}$ significantly increased in 24hr exposure on the uranyl nitrate and then decreased below the normal level after 3 days. The concentration of $Na^{+}\;and\;K^{+}$ in urines of the rats treated uranyl nitrate was less than that of the normal rats. The activities of $Na^{+}-K^{+}$ATPase decreased only in the group treated with high dose group of uranyl nitrate (30mg/kg BW) on the 3rd day but were not changed in the low dose groups(5 mg/kg BW and 15mg/kg BW).

• Journal of Radiation Protection and Research
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• v.15 no.2
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• pp.1-6
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• 1990

An attempt was made to test the possibility of a major role for the $Na^{+}-K^{+}$ adenosine triphosphatase (ATPase)system in the diuresis induced by uranyl nitrate(UN). Fisher 344 rats were intravenously injected with UN(5 mg/kg, 15 mg/kg and 30 mg/kg). Urinary excretion of $Na^{+}\;and\;K^{+}$ significantly increased in 24 h exposure on the UN and then decreased below the normal level 3 days after the treatment. $Na^{+}-K^{+}$ ATPase activity of kidney was significantly inhibited in high dosages of UN 15mg/kg and UN 30 mg/kg 3-5 days after injection. And then the recovery of the enzyme activity was observed within 5-10 days after injection, at which the regeneration of the tubular cells occurred.

• Toxicological Research
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• v.34 no.2
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• pp.143-150
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• 2018

It has been demonstrated that vanadate causes nephrotoxicity. Vanadate inhibits renal sodium potassium adenosine triphosphatase (Na, K-ATPase) activity and this is more pronounced in injured renal tissues. Cardiac cyclic adenosine monophosphate (cAMP) is enhanced by vanadate, while increased cAMP suppresses Na, K-ATPase action in renal tubular cells. There are no in vivo data collectively demonstrating the effect of vanadate on renal cAMP levels; on the abundance of the alpha 1 isoform (${\alpha}_1$) of the Na, K-ATPase protein or its cellular localization; or on renal tissue injury. In this study, rats received a normal saline solution or vanadate (5 mg/kg BW) by intraperitoneal injection for 10 days. Levels of vanadium, cAMP, and malondialdehyde (MDA), a marker of lipid peroxidation were measured in renal tissues. Protein abundance and the localization of renal ${\alpha}_1-Na$, K-ATPase was determined by Western blot and immunohistochemistry, respectively. Renal tissue injury was examined by histological evaluation and renal function was assessed by blood biochemical parameters. Rats treated with vanadate had markedly increased vanadium levels in their plasma, urine, and renal tissues. Vanadate significantly induced renal cAMP and MDA accumulation, whereas the protein level of ${\alpha}_1-Na$, K-ATPase was suppressed. Vanadate caused renal damage, azotemia, hypokalemia, and hypophosphatemia. Fractional excretions of all studied electrolytes were increased with vanadate administration. These in vivo findings demonstrate that vanadate might suppress renal ${\alpha}_1-Na$, K-ATPase protein functionally by enhancing cAMP and structurally by augmenting lipid peroxidation.

• The Korean Journal of Pharmacology
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• v.8 no.1
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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.

• Advances in Traditional Medicine
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• v.3 no.3
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• pp.129-132
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• 2003

The hypoglycemic and hypolipidaemic effects of fenugreek seeds (Trigonella foenum graecum) are well established. Owing to the wide spread use of the seeds by healthy individuals and by diabetic patients we wanted to test whether the seeds can affect biological systems such as membrane transport function. In the present study fenugreek seed polyphenols were extracted and their effect on erythrocyte membrane-bound sodium-potassium adenosine triphosphatase $(Na^+/K^+-ATPase)$ activity was studied in vitro. Fenugreek seed polyphenols inhibited $Na^+/K^+-ATPase$ in erythrocyte membrane of diabetic and normal subjects. Maximum inhibition was observed at $100\;{\mu}l$ of extract containing 0.75 mM gallic acid equivalents. The uncoupling of membrane ATPases in vitro suggest that polyphenols from fenugreek seeds may possess a positive inotropic effect.