Onishi H, Yamada Y, Ikebe M, Suzuki H, Watanabe S
J Biochem. 1978 Jan;83(1):129-35. doi: 10.1093/oxfordjournals.jbchem.a131883.
On studying the steady-state activity in 0.6 M KCl, it was found that Mg-ATPase of chicken gizzard myosin was identical with that of rabbit skeletal myosin in the pH-activity profile, Michaelis-Menten constant, and maximum velocity. As regards the "initial burst" of ATP splitting in the presence of Mg (0.6 M KCl), it was found that gizzard and skeletal myosins were identical both in the size of the initial burst and in the velocity-ATP concentration relationship. The only difference we observed was that the Ca- and EDTA-ATPase activities of gizzard myosin were, as reported by other investigators, approximately one-half to one-third of those of skeletal myosin, although the pH-activity profiles for the ATPase of gizzard myosin was essentially the same as that of skeletal myosin.
在研究0.6M氯化钾中的稳态活性时，发现鸡胗肌球蛋白的镁 - ATP酶在pH - 活性曲线、米氏常数和最大速度方面与兔骨骼肌肌球蛋白相同。关于在镁存在下（0.6M氯化钾）ATP分解的“初始爆发”，发现鸡胗肌球蛋白和骨骼肌肌球蛋白在初始爆发的大小以及速度 - ATP浓度关系方面都是相同的。我们观察到的唯一差异是，正如其他研究者所报道的，鸡胗肌球蛋白的钙 - 和EDTA - ATP酶活性约为骨骼肌肌球蛋白的二分之一到三分之一，尽管鸡胗肌球蛋白ATP酶的pH - 活性曲线与骨骼肌肌球蛋白的基本相同。
