Schloss J A, Goldman R D
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4484-8. doi: 10.1073/pnas.76.9.4484.
A high molecular weight protein (HMWP) with properties similar to those of both actin-binding protein (ABP) and filamin has been isolated from cultured baby hamster kidney (BHK-21) cells. The protein was present in an actomyosin-depleted sucrose extract of the cells and was eluted, upon gel chromatography on Sepharose 4B, near the void volume. The subunit migration on sodium dodecyl sulfate/polyacrylamide gels and the amino acid composition of HMWP were similar to those of ABP and filamin. HMWP bound to and crosslinked F-actin from rabbit muscle, as shown by the formation of a gel that was sedimented with low-speed centrifugation. This interaction was insensitive to temperature and low concentrations of calcium ions, although it may depend on the presence of myosin. Observation of thin sections of the actin-HMWP gel revealed crosslinked complexes of laterally aggregated actin filaments. The axial period of the dense crosslinks was 34 nm. The HMWP may be involved in regulation of microfilament organization.
从培养的幼仓鼠肾（BHK-21）细胞中分离出了一种高分子量蛋白质（HMWP），其性质与肌动蛋白结合蛋白（ABP）和细丝蛋白的性质相似。该蛋白质存在于细胞的肌动球蛋白耗尽的蔗糖提取物中，在Sepharose 4B上进行凝胶色谱分析时，在空体积附近被洗脱。HMWP在十二烷基硫酸钠/聚丙烯酰胺凝胶上的亚基迁移和氨基酸组成与ABP和细丝蛋白相似。HMWP与兔肌肉中的F-肌动蛋白结合并交联，低速离心沉淀形成凝胶即可证明这一点。这种相互作用对温度和低浓度钙离子不敏感，尽管它可能依赖于肌球蛋白的存在。对肌动蛋白-HMWP凝胶薄片的观察显示，横向聚集的肌动蛋白丝形成了交联复合物。密集交联的轴向周期为34纳米。HMWP可能参与微丝组织的调节。
