Lehman W
Department of Physiology, Boston University School of Medicine, MA 02118.
Biochim Biophys Acta. 1989 Jun 13;996(1-2):57-61. doi: 10.1016/0167-4838(89)90094-0.
A 35 kDa protein present in vertebrate smooth muscle and capable of binding to purified actin does not appear to be a constituent of smooth-muscle thin filaments in vivo; instead, it is more likely to be a component easily solubilized from particulate material which then spuriously interacts with actin.
一种存在于脊椎动物平滑肌中、能够与纯化肌动蛋白结合的35 kDa蛋白质,在体内似乎并非平滑肌细肌丝的组成成分;相反,它更有可能是一种易于从颗粒物质中溶解出来的成分,然后与肌动蛋白发生假性相互作用。