닭고기의 근원섬유 단백질에 관한 연구 -2. 골격근 부위별로 추출한 근원섬유, 액토미오신 및 미오신의 ATPase 활성 비교- Studies on the Myofibrillar Proteins from Chicken Muscle -2. Comparison of ATPase Activity in Myofibril, Actomyosin and Myosin Extracted from Leg and Pectoral Skeletal Muscle원문보기
Some biological activities showed as ATPase activity of myofibril, actomyosin and myosin extracted from chicken leg and pectoral skeletal muscle were investigated. The $Mg^{+2}$-ATPase activity at 0.05 M KCl were 0.82, 0.38 and 0.11 ${\mu}mole$ Pi/mg protein/min. in actomyosin,...
Some biological activities showed as ATPase activity of myofibril, actomyosin and myosin extracted from chicken leg and pectoral skeletal muscle were investigated. The $Mg^{+2}$-ATPase activity at 0.05 M KCl were 0.82, 0.38 and 0.11 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle while 0.71, 0.32 and 0.08 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from leg muscle. EDTA-ATPase activity at 0.6M KCl were 0.80, 0.42 and 0.40 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle. In case of leg muscle, that activity was noted as 0.69, 0.33 and 0.28 ${\mu}mole$e Pi/mg protein/min in proteins. ATPase activity of myosin from leg and pectoral muscle were inhibited in 10% at a higher concentration of $Mg^{+2}$ than molar concentration of EDTA, and the ATPase activity was increased to 400% compared with control at $10^{-3}M$ of $Ca^{+2}$. Actomyosin from pectoral muscle was solubilized at 0.1 M KCl above and that from leg muscle was solubilized at 0.15 M KCl above. In case of myosin, pectoral muscle was solubilized at 0.25M KCI above and leg muscle was solubilized at 0.30M KCl above.
Some biological activities showed as ATPase activity of myofibril, actomyosin and myosin extracted from chicken leg and pectoral skeletal muscle were investigated. The $Mg^{+2}$-ATPase activity at 0.05 M KCl were 0.82, 0.38 and 0.11 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle while 0.71, 0.32 and 0.08 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from leg muscle. EDTA-ATPase activity at 0.6M KCl were 0.80, 0.42 and 0.40 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle. In case of leg muscle, that activity was noted as 0.69, 0.33 and 0.28 ${\mu}mole$e Pi/mg protein/min in proteins. ATPase activity of myosin from leg and pectoral muscle were inhibited in 10% at a higher concentration of $Mg^{+2}$ than molar concentration of EDTA, and the ATPase activity was increased to 400% compared with control at $10^{-3}M$ of $Ca^{+2}$. Actomyosin from pectoral muscle was solubilized at 0.1 M KCl above and that from leg muscle was solubilized at 0.15 M KCl above. In case of myosin, pectoral muscle was solubilized at 0.25M KCI above and leg muscle was solubilized at 0.30M KCl above.
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