Murayama T, Nakauchi Y, Kimura S, Maruyama K
Department of Biology, Faculty of Science, Chiba University.
J Biochem. 1989 Feb;105(2):323-6. doi: 10.1093/oxfordjournals.jbchem.a122661.
Binding of native connectin (2,100 kDa fragment of alpha-connectin) to myosin filaments was investigated using a sedimentation technique and densitometric estimations of the separated proteins. In the presence of 60 mM KCl and 5 mM phosphate buffer, pH 7.0, as much as 1.5 mol of connectin was bound to 1 mol of myosin, suggesting that some 150 connectin filaments bound to a single myosin filament of approximately 0.5 micron in length. This value was much more than the ratio found in muscle (12:1). It appeared that C protein did not affect the binding of connectin to myosin filaments.
利用沉降技术和对分离蛋白质的光密度测定,研究了天然连接蛋白(α-连接蛋白的2100 kDa片段)与肌球蛋白丝的结合情况。在含有60 mM氯化钾和5 mM磷酸盐缓冲液(pH 7.0)的条件下,1摩尔肌球蛋白可结合多达1.5摩尔连接蛋白,这表明约150条连接蛋白丝与一条长度约为0.5微米的单个肌球蛋白丝结合。该值远高于在肌肉中发现的比例(12:1)。似乎C蛋白不影响连接蛋白与肌球蛋白丝的结合。