Yamaguchi M, Robson R M, Stromer M H
J Cell Biol. 1983 Feb;96(2):435-42. doi: 10.1083/jcb.96.2.435.
Canine and feline cardiac Z-lines and Z-rods were examined by electron microscopy before and after digestion of muscle fibers with Ca2+-activated protease (CAF). Removal by CAF of electron-dense material which covers Z-lines and Z-rods exposed interdigitating longitudinal filaments (6-7 nm in diameter) apparently continuous with thin filaments of the respective I-bands. The newly exposed longitudinal filaments of CAF-treated Z-lines and of CAF-treated Z-rods bound heavy meromyosin and therefore are actin. The width of Z-lines and length of Z-rods are determined by the amount of overlap of actin filaments of opposite polarity. The oblique filaments in Z-lines and Z-rods are responsible for the perpendicular periodicity of Z-lines and Z-rods, and are attributed to alpha-actinin.
在用钙离子激活蛋白酶(CAF)消化肌纤维前后,通过电子显微镜对犬类和猫类心脏的Z线和Z棒进行了检查。CAF去除覆盖Z线和Z棒的电子致密物质后,暴露出相互交错的纵向细丝(直径6-7纳米),这些细丝显然与各自I带的细肌丝相连。经CAF处理的Z线和经CAF处理的Z棒新暴露的纵向细丝结合了重酶解肌球蛋白,因此是肌动蛋白。Z线的宽度和Z棒的长度由相反极性的肌动蛋白丝的重叠量决定。Z线和Z棒中的斜向细丝决定了Z线和Z棒的垂直周期性,并且归因于α-辅肌动蛋白。