• Title/Summary/Keyword: $Mg^{2+}$-ATPase

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Studies on the ATPases of Fragmented Sarcoplasmic Reticulum of Rabbit Skeletal Muscle (家兎골격근小胞體切片의 ATPase 에 관한 硏究)

  • Ha, Doo-Bong;Eunsook Song;Park, Hee-Soon
    • The Korean Journal of Zoology
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    • v.17 no.2
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    • pp.93-102
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    • 1974
  • Fragmente dsarcoplasmic reticulum of rabbit skeletal muscle was prepared and biochemical properties of its ATPase activity were studied. The ATPase of the fragments could be distinguished as $Mg^++ - ATPase and (Mg^++ - Ca^++)$-ATPase. The activity of $(Mg^++ - Ca^++)$-ATPase was predominant over that of $Mg^++$-ATPase in the temperature range of $0 \\sim 40^\\circ C$ and in the pH 6.4$\\sim$7.6. At higher temperatures the predominance of $(Mg^++ - Ca^++)$-ATpase was far greater. The apparent energies of activation were 14 kcal/mole for $Mg^++$-ATPase, 21kcal/mole for $(Mg^++ - Ca^++)$-ATPase, and 18kcal/mole for total ATPase. Changes in pH and Mg concentration did not alter the energies of activation of these ATPases. The Km values of these ATPases were found to be 0.36 mM for $Mg^++$-ATPase, 2.20 mM for $(Mg^++ - Ca^++)$-ATpase, and 0.86 mM for total ATPase.

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Effects of Ijingtang fractions on activities of NaK ATPase and Ca ATPase in rat brain synaptosome (이진탕 분획엑스가 synaptosomal NaK ATPase와 Ca ATPase의 활성도에 미치는 영향)

  • Jo, Yeong-Uk;Han, Seung-Ho;Kim, Chang-Ju;Min, Byeong-Il;Lee, Tae-Hui;Yun, Sang-Hyeop;O, Su-Myeong
    • The Journal of Korean Medicine
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    • v.18 no.1
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    • pp.198-207
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    • 1997
  • To explore the action mechanism of Ijintang in the brain, the authors investigated the effects of Ijintang fractions on MgNaK ATPase and MgCa ATPase in rat brain synaptosomes prepared from cerebral cortex. The activities of MgNaK ATPase and MgCa ATPase were assayed by the level of inorganic phosphate liberated from the hydrolysis of ATP. Fraction WH-95-7 at the concentration of $10^{-2}%$ decreased the activity of MgNaK ATPase about 34.1% and also reduced the activity of MgCa ATPase about 49.3% But, other fractions (WB-95-7, WC-95-7, MB-95-7, MC-95-7, MH-95-7) did not significantly changed the activities of the MgNaK ATPase and MgCa ATPase The decreased activity of MgNaK ATPase by WH-95-7 will decrease the rate of $Ca^{2+}$ efflux, probably via an Na-Ca exchange mechanism and will increase the rate of $Ca^{2+}$ entry by the depolarization of nerve terminals. The reduced activity of MgCa ATPase by WH-95-7 will result in the decreased efflux of $Ca^{2+}$. As a conclusion, it can be speculated that lithium elevates the intrasynaptosomal $Ca^{2+}$ concentration via inhibition of the activities of MgNaK ATPase and MgCa ATPase. and this increased $[Ca^{2+}]i$ will cause the release of neurotransmitters.

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Inhibition of Microsomal $H^+\;-\;ATPase$ Prepared from Tomato Roots by Various Anions (음이온에 의한 토마토 뿌리조직 마이크로솜 $H^+-ATPase$ 활성 저해)

  • Shin, Dae-Seop;Kim, Young-Kee
    • Applied Biological Chemistry
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    • v.44 no.2
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    • pp.67-72
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    • 2001
  • $H^+-ATPase$ located on plasma and vacuolar membranes play major roles in various cellular physiological processes. In order to investigate the physiological roles of $H^+-ATPase$, microsomes were prepared from tomato roots and the effects of various anions were measured on the activities of $H^+-ATPase$. $H^+-ATPase$ was inhibited by various anions. Citrate and phosphate were chosen to investigate detailed inhibitory mechanisms on $H^+-ATPase$ since they showed different levels of inhibition. Inhibitory effect of citrate was observed at the concentrations above 3 mM. When 20 mM citrate was added, the ATPase activity was decreased by 50-60%. However, the inhibitory effect of citrate was decreased by increasing the concentration of$Mg^{2+}$ The citrate-induced inhibited activity was recovered by the addition of $Mg^{2+}$ Addition of 7 mM $Mg^{2+}$ completely removed the inhibitory effect of citrate and the activity recovered to the level of the control experiment. These results imply that citrate chelates $Mg^{2+}$ and thus inhibits $H^+-ATPase$. Meanwhile, the inhibitory effect of phosphate was observed at the concentration above 3 mM and the activity was decreased by 50% in the presence of 30 mM phosphate. Further addition of $Mg^{2+}$ showed no recovery on the activity. These results imply that the inhibitory effect of phosphate is not dependent upon the concentration of $Mg^{2+}$.

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A BIOCHEMICAL STUDY OF $Ca^{++}$-ATPASE AND $Mg^{++}$-ATPASE ACTIVITY IN HUMAN DENTAL PULP (치수에서 $Ca^{++}$-ATPase와 $Mg^{++}$-ATPase의 활성도에 관한 실험적 연구)

  • Hwang, In-Sung;Lee, Jong-Gap
    • Journal of the korean academy of Pediatric Dentistry
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    • v.10 no.1
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    • pp.139-147
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    • 1983
  • This study was undertaken to evaluate the physiological roles & mechanism of $Ca^{++}$-ATPase & $Mg^{++}$-ATPase in human dental pulp. Each specimen of dental pulp was obtained from the freshly extracted, freeze-dried 242 teeth. $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were measured by the release of inorganic phosphate & protein with Spectrophotometer. The results were as follows; 1. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significantly increased in developing teeth. 2. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significantly decreased in nonvital teeth. 3. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significant decreased in deciduous teeth. 4. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity didn't have relation with dental caries. 5. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase were activated by either $Ca^{++}$ alone or $Mg^{++}$ alone.

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Seasonal Variation in the $Na^+$,$K^+$-ATPase Activity in Frog (Rana dybowskii) Brain (개구리 뇌에서 $Na^+$,$K^+$- ATPase 특성의 계절적 변화)

  • 김미승;임욱빈
    • The Korean Journal of Zoology
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    • v.38 no.4
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    • pp.449-456
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    • 1995
  • Seasonal changes in the activity and charaderistics of brain Na+, K+-ATPase and Mg2+-AWase were investigated in frog (Rana dybowskii) The brain Na+, K+-ATPase adivity during hibernation was similar to that in active period in frogs. The Na+, K+-AWase activity increased in December and March, when the frogs enter into and awake from the hibernation. Over 5-35$^{\circ}C$ temperature range, Na+, K+-ATPase showed non4inear Arrhenius kinetics throughout the year. The brain Mg2+-ATPase activity decreased during hibernation, but markedly increased in March. The Arrhenius plots for Mg2+-AWase activity were linear in frogs both in torpid and active state. The ratio of Na+, K+-AWase activity at 15~C to at 35~C did not change during hibernation. The sensitivity of Na+, K+-AWase to ouabain was also unchanged throughout the year. These results indicate that the activity and charaderistics of brain Na+, K+-AWase remain unchanged during hobernadon in frog.

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The Effect of $Mg^#$, $Ca^#$, $Na^+$, $K^+$ and Creatine Phosphate on the ATPase Activity of Microsomal Fraction from Rabbit Uterus (가토자궁근(家兎子宮筋)에서 분리(分離)한 Microsome 분획내(分劃內) Adenosinetriphosphatase 활성도(活性度)에 미치는 $Mg^#$, $Ca^#$, $Na^+$, $K^+$ 및 Creatine phosphate의 영향(影響))

  • Choi, Sin-Jyoung
    • The Korean Journal of Pharmacology
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    • v.2 no.2
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    • pp.35-42
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    • 1966
  • The author investigated the effect of $Mg^#$, $Ca^#$, $Na^+$, $K^+$ and creatine phosphate on the ATPase activity of microsomal fraction isolated from rabbit uterus and obtained the following results : 1) The uterine microsomal fraction contained the $Na^+-$ and $K^+-$ activated ATPase in the presence of $Mg^#$. The ATPase activity increased with protein content in the fraction. 2) The maximum ATPase activity was obtained at $Na^+$ and $K^+$ concentraction of 100 mM respectively. 3) In the absence of $Mg^#$, the ATPase was not activated by $Na^+$ and $K^+$, but inhibited. 4) Car stimulated the $Na^+-$ and $K^+-$ activated ATPase in the presence of $Mg^#$. However, in the absence of $Mg^#$, the ATPase was not activated by $Ca^#$. 5) The $K^+-$ activated ATPase activity was greater than the $Na^+-activated$ ATPase under all conditions. 6) The $Na^+-$ and $K^+$ activated ATPase activity was increased by addition of creatine phosphokinase and creatine phosphate to the reaction mixture.

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ATPase Activity and Solubility of Actomyosin Extracted from Muscle of Silky Fowl (오골계에서 추출한 Actomyosin 의 ATPase 활성 및 용해도)

  • 정인철;문윤희
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.23 no.5
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    • pp.827-831
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    • 1994
  • Investigation on the extractability, Mg2+-, Ca2+ , EDTA-ATPase activity and solubility of actomyosin prepared from leg and breast muscle of silky fowol were as follows. The extractability of actomyosin in leg and breast muscle was 779mg/100g and 1, 318mg/100g respectively, breast muscle was higher than leg muscle . Mg2+-ATPase activity of actomyosin was high inionic strength 0.02-0.10 and Mg2+ATPase activity of low ionic strength was higher than high ionic strength not related to the part. Ca2+ ATPase activity was high in ionic strength 0.05-0.13, the activity of leg muscle was higher that breast muscle. And EDTA-ATPase activity showed low in low ionic strength and showed high in high ionic strength, and increased greatly depend ionic strength up to 0.4. The solubility of actomyosin was not different in leg and breast muscle , the solution started in KCI concentration of 0.3M and ended in DCI concentration of 0.4M.

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Determination of $K^+-, Ca^{2}+- and Mg^{2+}-$ATPase activities in Fish Muscle Protein by ATPase Biosensor (ATPase 센서를 이용한 어류근육 단백질의 $K^+-, Ca^{2}+- 및 Mg^{2+}-$ ATPase 활성의 측정)

  • 천병수;김희경
    • KSBB Journal
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    • v.11 no.5
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    • pp.518-523
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    • 1996
  • The sensor to determine ATPase activities was consisted of an immobilized enzyme membrane(purine nucloside phosphoryrase and xanthine oxidase) and an oxygen electrode. The proposed sensor was used for the determination of $K^+-, Ca^{2}+- and Mg^{2+}-$ATPase activities in several fish muscle proteins such as Thunnus albacares(Yellowfin tuna), Tetrapturus audax(Striped marlin), Prognichthys agoo(Japanese flyingfish), and Cypvinus carpio(Carp). $K^+-, Ca^{2}-$ATPase activities measured by the proposed sensor system were in good agreement with the results obtained by a conventional colorimetric assay. One cycle of assay could be completed within 3mlnutes.

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Changes in the $Ca^{2+}$-, $Mg^{2+}$- dependent Adenosine Triphosphatase Activity and Ultrastructure of Marine Fishes by Partial Freezing II. Changes in ATPase Activity of Yellowtail Actomyosin during Cold Storage (해산어의 부분동결에 의한 $Ca^{2+}$-, $Mg^{2+}$- dependent Adenosine Triphosphatase 활성 및 근섬유의 미세구조 변화 II. 저온저장에 의한 방어 Actomyosin ATPase의 활성변화)

  • 박찬성;최경호
    • 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.

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Changes in the $Ca^{2+}-,\;Mg^{2+}-dependent$ Adenosine Triphosphatase Activity and Ultrastructure of Marine Fishes by Partial Freezing -I. Denaturation of Yellowtail Myofibrillar ATPase During Cold Storage- (해산어의 부분동결에 의한 $Ca^{2+}-,\;Mg^{2+}-dependent$ Adenosine Triphosphatase 활성 및 근섬유의 미세구조의 변화 -I. 저온저장에 의한 방어 근원섬유 단백질의 변성-)

  • Choi, Kyoung-Ho;Park, Chan-Sung
    • 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 $Ca^{2+}-\;and\;Mg^{2+}-ATPase$.

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