[兔骨骼肌α-辅肌动蛋白的结构域组织]

[Domain organization of alpha-actinin from the rabbit skeletal muscle].

作者信息

Kuridze K Sh, Ven'iaminov S Iu, Simonidze M Sh, Nadirashvili N Sh, Zaalishvili M M

出版信息

Biokhimiia. 1988 Jun;53(6):899-904.

Abstract

Limited trypsinolysis of native alpha-actinin by trypsin was carried out. This procedure resulted in the formation of two large fragments with Mr of 30 and 70 kD which cover almost the whole subunit of alpha-actinin. Using the sedimentation equilibrium method, it was demonstrated that the bisubunit structure of alpha-actinin is provided for by C-terminal fragments of the subunits. Data from circular dichroism analysis suggest that the fragments formed are independent structural units, i.e., domains.

摘要

用胰蛋白酶对天然α-肌动蛋白进行了有限的胰蛋白酶解。该过程产生了两个分子量分别为30 kD和70 kD的大片段，它们几乎覆盖了α-肌动蛋白的整个亚基。使用沉降平衡法证明，α-肌动蛋白的双亚基结构是由亚基的C末端片段提供的。圆二色性分析数据表明，形成的片段是独立的结构单元，即结构域。