Lubit B W, Schwartz J H
J Cell Biol. 1980 Sep;86(3):891-7. doi: 10.1083/jcb.86.3.891.
We elicited antibodies in rabbits to actin purified from body wall muscle of the marine mollusc, Aplysia californica. We found that this antiactin has an unusual specificity: in addition to reacting with the immunogen, it recognizes cytoplasmic vertebrate actins but not myofibrillar actin. Radioimmunoassay showed little or no cross-reaction with actin purified from either chicken gizzard or rabbit skeletal muscle. Immunocytochemical studies with human fibroblasts and L6 myoblasts revealed intense staining of typical cytoplasmic cables. Myofibrils were not stained after treatment of human and frog skeletal muscle with the antibody, although the distribution of immunofluorescence suggested that cytoplasmic actin is associated with membrane systems in the muscle fiber. The antibody may therefore be especially suited for studying the localization of cytoplasmic actin in skeletal muscle cells even in the presence of a great excess of the myofibrillar form.
我们在兔子体内诱导产生了针对从海洋软体动物加州海兔体壁肌肉中纯化出的肌动蛋白的抗体。我们发现这种抗肌动蛋白具有不同寻常的特异性:除了与免疫原发生反应外,它还能识别脊椎动物的细胞质肌动蛋白,但不能识别肌原纤维肌动蛋白。放射免疫分析表明,它与从鸡胗或兔骨骼肌中纯化出的肌动蛋白几乎没有交叉反应。对人成纤维细胞和L6成肌细胞进行的免疫细胞化学研究显示,典型的细胞质束呈现强烈染色。用该抗体处理人和青蛙的骨骼肌后,肌原纤维未被染色,尽管免疫荧光的分布表明细胞质肌动蛋白与肌纤维中的膜系统相关。因此,即使存在大量的肌原纤维形式,该抗体可能特别适合用于研究骨骼肌细胞中细胞质肌动蛋白的定位。