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문윤희(Y . H . Moon),황칠성(C . S . Hwang),양융(R . Yang) 한국축산학회 1984 한국축산학회지 Vol.26 No.1
The extraction of actomyosin from skeletal muscle of mammals and avians. Biochemical activities and the effect of EGTA on Mg-activated ATPase activity of actomyosin were compared function of animal species. Myosin was first released during the extraction followed by actin, which upon the release, formed actomyosin thus indicating a certain difference in compactness in filamental lattice and filamental integrity. And 125 micro M EGTA inhibited Mg-ATPase activity indicating a common component of troponin regardless the animal species and the duration of extraction of this substance. The Mg-enhanced ATPase activity of actomyosin demonstrated a biphasic response, a high activity at low ionic strength and low activity at a high ionic strength. The dissociation of myosin and actin from actomyosin was observed to be more difficult when the actomyosin was originated from cattle or swine when corupared with that of rabbit; even though the same method was applied for the extraction of the amount of myosin contained in actomysin varied remarkably among the apecies.