Miyahara M, Kishi K, Noda H
J Biochem. 1980 May;87(5):1341-5. doi: 10.1093/oxfordjournals.jbchem.a132873.
F-Protein has an amino acid composition distinctively different from those of myofibriller proteins so far reported to be of similar chain weight: M-protein component II, alpha-actinin, and AMP deaminase. Its molecular weight was estimated to be 121,000 by sedimentation equilibrium in 0.3 M KCl, 10 mM potassium phosphate, pH 6.5. Its binding to myosin was inhibited by C-protein. It reduced the effect of C-protein on the assembly reaction of myosin in vitro.
F-蛋白的氨基酸组成与迄今报道的链重相似的肌原纤维蛋白截然不同：M-蛋白组分II、α-辅肌动蛋白和AMP脱氨酶。在0.3M KCl、10mM磷酸钾、pH 6.5条件下，通过沉降平衡法估计其分子量为121,000。其与肌球蛋白的结合受到C-蛋白的抑制。它降低了C-蛋白对肌球蛋白体外组装反应的影响。
