Bennett J P, Cross R A, Kendrick-Jones J, Weeds A G
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
J Cell Biol. 1988 Dec;107(6 Pt 2):2623-9. doi: 10.1083/jcb.107.6.2623.
We have purified a polyclonal antibody by affinity chromatography which binds specifically to the phosphorylated form of the regulatory light chain (Mr = 20,000) of smooth muscle myosin. This antibody does not stain relaxed, permeabilized smooth muscle cells isolated from guinea pig taenia coli. However, when these cells were stimulated to contract with CaCl2 (100 microM) and ATP (1 mM), the immunofluorescence staining was localized in a series of transverse bands. This distribution of activated myosin appears to reflect an underlying structural organization of the smooth muscle cell cytoskeleton into mechanically coupled contractile zones.
我们通过亲和层析纯化了一种多克隆抗体,该抗体能特异性结合平滑肌肌球蛋白调节轻链(分子量 = 20,000)的磷酸化形式。这种抗体不会对从豚鼠结肠带分离出的松弛、透化的平滑肌细胞进行染色。然而,当用氯化钙(100微摩尔)和ATP(1毫摩尔)刺激这些细胞收缩时,免疫荧光染色定位于一系列横向带中。活化肌球蛋白的这种分布似乎反映了平滑肌细胞细胞骨架在机械耦合收缩区的潜在结构组织。