• Title/Summary/Keyword: frog skeletal muscle

검색결과 6건 처리시간 0.02초

Cortisone 및 Calcium이 국소마취약의 Acetylcholine 근련축억제효과에 미치는 영향

  • 배유홍;함종대;이상신
    • 대한치과의사협회지
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    • 제12권6호
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    • pp.419-423
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    • 1974
  • The authors have investigated the roles of cortisone and calcium on the depressive effects of local anesthetics on the acetylcholine-induced skeletal muscle contraction in frog. The results are as follows. 1. Tetracaine, cocaine, lidocaine and procaine decreased the acetylcholine-induced skeletal muscle contraction. 2. Cortisone increased the depressive effects of local anesthetics on the acetyl-choline-induced skeletal muscle contraction. 3. There was a tendency that in high calcium concentration, the depressive effects of cocaine and lidocaine on acetylcholine-induced skeletal muscle contraction were increased.

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인삼추출물이 흥분성세포의 막전압에 미치는 영향 (Effects of Ginseng Extract on Excitable Cell Membrane Potential)

  • 정진모;백광세;남택상;김인교;강두희
    • The Korean Journal of Physiology
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    • 제15권1호
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    • pp.3-8
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    • 1981
  • Studies have been conducted to test the effect of Ginseng alcohol extract on the membrane potentials of frog skeletal muscle. The gastrocnemius muscle was isolated and placed in a chamber containing the Clark-frog Ringer solution. Membrane potentials were recorded using microelectrodes filled with 3 M KCI and muscle was electrically stimulated to obtain action potential. Changes in both the action potential and the resting membrane potential were observed after adding an appropriate amount of Ginseng alcohol extract in the perfusing Ringer solution. The results obtained from 346 muscle cells are summarized as follows : 1) The average resting membrane potential of the normal frog gastrocnemius muscle cell was -92.8 mV and the peak of the action potential reached at 29.8 mV. 2) Both the resting membrane potential and the peak of the action potential decreased by Ginseng alcohol extract, the effect being proportional to the dose of Ginseng alcohol extract. 3) The resting membrane potential and the peak of the action potential continuously decreased until about 40 min after Ginseng addition and leveled off thereafter. The potentials recovered to its original value after Ginseng was washed out. 4) The resting membrane potential was more sensitive to the Ginseng alcohol extract than was the action potential. These results strongly suggest that Ginseng alcohol extract increases both the $Na^+$ and $K^+$ permeability in the skeletal muscle cell membrane.

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개구리 세포막에 대한 Racemic Ketamine의 영향 (Effects of Racemic Ketamine on Excitable Membranes of Frog)

  • 이종화
    • 대한약리학회지
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    • 제27권2호
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    • pp.99-108
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    • 1991
  • Racemic ketamine을 사용하여 개구리의 좌골신경 및 toe muscle에 대한 작용을 관찰하였다. 실험방법으로는 214 mM sucrose을 사용하여 서로 다른 두 종류의 투여 방법으로 세포막의 활동 전압에 대한 영향을 electric recording으로 관찰하였다. 즉, intracellular 투여는 single sucrose gap technique으로, extracellar 투여는 double sucrose gap technique을 사용하였으며 그 실험 결과는 아래와 같았다. 1. Racemic ketamine은 개구리의 좌골신경 및 toe muscle의 활동전압을 intracellular 및 extracellular 투여시 모두 의의 있게 억제하였다. 2. 개구의 toe muscle에서 $K^+$-수축을 억제하였다. 3. naloxone은 ketamine의 억제작용을 완전히 차단하지는 못하였다.

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Actomyosin $Ca^{++}$ Activated Adenosinetriphosphatase 활성도에 대한 pH 및 온도의 영향 (pH-Temperature Dependence of the Ca-ATPase Activity in Actomyosin Systems of Rabbit and Frog Skeletal muscle)

  • 김희중;황애란;박양생;강두희
    • The Korean Journal of Physiology
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    • 제11권2호
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    • pp.1-7
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    • 1977
  • The activity of the $Ca^{++}$ activated adenosinetriphosphatase (Ca-ATPase) of actomyosin systeme of rabbit and frog skeletal muscle has been studied at varying pH and temperature. The PH optima of the Ca-ATPase activity of the rabbit actomyosin was rather broad. Over the temperature range of $16-36^{\circ}C$ activity of the enzyme was not appreciably changed between pH 6.4-8.5; below and above which it rapidly reduced. The pH at the inflection point of the enzyme activity increased as temperature decreased, showing the ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ of approximately $-0.018\;unit/^{\circ}C$. Consequently, $(OH^-)/(H^+)$ ratio at the inflection point was constant regardless of assay temperature. In the frog actomyosin systems the Ca-ATPase activity was not apparently altered between PH 6.4-7.0 when the incubation temperature was $15{\sim}30^{\circ}C$. Outside of this range of pH, however, the enzyme activity was dramatically decreased. The pH of the inflection point changed inversely with temperature. ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ at the acidic side was approximately $-0.018\;unit/^{\circ}C$, whereas that at the alkaline side it was about $-0.037\;unit/^{\circ}C$. The Arrhenius Plot on the Ca-ATPase activity at constant $(OH^-)/(H^+)$ ratio of 1.0 was not linear, but showed break at arround $20^{\circ}C$ for both rabbit and frog actomyosin Preparations. From these results it was speculated that pH dependence of Ca-ATPase activity of rabbit actomyosin systems might reflect titrations of histidine-imidazole and -SH groups, and that of the frog actomyosin represents titrations of histidine-imidazole and lysyllysine ${\alpha}-NH_2$ groups.

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평지방막에 융합된 골격근의 single ATP-sensitive K+ channel의 이온투과성에 대한 연구 (Permeability properties of skeletal muscle ATP-sensitive K+ channels reconstituted into planar lipid bilayer)

  • 류판동
    • 대한수의학회지
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    • 제32권4호
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    • pp.543-553
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    • 1992
  • Properties of unitary ATP-sensitive $K^+$ channels were studied using planar lipid bilayer technique. Vesicles were prepared from bullfrog (Rana catesbeiana) skeletal muscle. ATP-sensitive $K^+$ (K (ATP)) channels were identified by their unitary conductance and sensitivity to ATP. In the symmetrical solution containing 200mM KCI, 10mM Hepes, 1mM EGTA and pH 7.2, single K (ATP) channels showed a linear current-voltage relations with slight inward rectification. Slope conductance at reversal potential was $60.1{\pm}0.43$ pS(n=3)). Micromolar ATP reversibly inhibited the channel activity when applied to the cytoplasmic side. In the range of -50~+50 mV, the channel activity was not voltage-dependent, but the channel gating within a burst was more frequent at negative voltage range. Varying the concentrations of external/internal KCl(mM) to 40/200, 200/200, 200/100 and 200/40 shifted reversal potentials to $-30.8{\pm}2.9$(n=3), $-1.1{\pm}2.7$(n=3), 10.5 and 30.6(mV), respecrivety. These reversal potentials were close to the expected values by the Nernst equation, indicating nearly ideal selectivity for $K^+$ over $Cl^-$. Under bi-ionic conditions of 200mM external test ions and 200mM internal $K^+$, the reversal potentials for each test ion/K pair were measured. The measured reversal potentials were used for the calculation of the releative permeability of alkali cations to $K^+$ ions using the Goldman-Hodgkin-Katz equation. The permeability sequence of 5 cations relative to $K^+$ was $K^+$(1), $Rb^+$(0.49), $Cs^+$(0.27), $Na^+$(0.027) and $Li^+$(0.021). This sequence was recognized as Eisenman's selectivity sequence IV. In addition, modelling the permeation of $K^+$ ion through ATP-sensitive $K^+$ channel revealed that a 3-barrier 2-site multiple occupancy model can reasonably predict the observed current-voltage relations.

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Properties of Single $K^{+}$ Channels of Skeletal Muscle Incorporated into Planar Lipid Bilayer

  • Park, Jin-Bong;Kim, Hee-Jeong;Cho, Myung-Haing;Lee, Hang;Park, Hong-Ki;Lee, Mun-Han;Ryu, Pan-Dong
    • The Korean Journal of Physiology
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    • 제29권1호
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    • pp.13-27
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    • 1995
  • single $K^{+}$ channels of skeletal muscle from the rat and frog were into planar lipid bilayers and their properties were studied. Fusion was induced by an osmotic gradient. Of the four types of $K^{+}$ channels recorded, the two most frequently observed were a voltage and $Ca^{2+}-activated$ $K^{+}$ channel and a $K^{+}$ channel with a prominent conductance substate. The first $K^{+}$ channel was identified as the large $Ca^{2+}-activated$ $K^{+}$ (BK) channel because the open-state probability was increased with depolarization (e-fold change per $10.6{\pm}3.5$ mV, n=8) and internal $Ca^{2+}$ (half-activation at $16.7{\pm}3.8$ mV, n=8, pCa 4) and its conductance was large ($247{\pm}4.9$ pS, n=24 in 0.1 M KCI). Lifetime distributions of open- and closed-states could be fitted with single exponentials of several milliseconds. The mean open- and closed-lifetimes were linearly dependent on the intracellular $[Ca^{2+}]$ and $1/[Ca^{2+}]$, respectively. The second $K^{+}$ channel showed a conductance substate at $30{\sim}60%$ of the open state. Its current-voltage relation was linear in the range of $-80\;{\sim}\;+80\;mV$. The slope conductance of the substate and open-state were 40 and 144 pS in 0.2 M KCl, respectively. The channel was highly selective for $K^{+}$ over Cl. The open-state probability was weakly voltage-dependent (e-fold change per 35 mV. The lifetime distributions of open- and closed-states were fitted with two exponentials and the major gating occurred slowly at several hundred milliseconds. Based on the above results, we think the second type of $K^{+}$ channel is the sarcoplasmic reticulum $K^{+}$ (SRK) channel. In addition, both types of channel were also incorporated into the lipids extracted from the skeletal muscle. The channel properties recorded in the bilayers termed from synthetic and extracted lipids were qualitatively similar. Our data indicate that BK and SRK channels are rich in the skeletal muscle and their properties and regulation could be effectively studied in planar lipid bilayer.

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