ACTIN POLYMERIZABILITY IS INFLUENCED BY PROFILIN, A LOW-MOLECULAR WEIGHT PROTEIN IN NON-MUSCLE CELLS
ACTIN POLYMERIZABILITY IS INFLUENCED BY PROFILIN, A LOW-MOLECULAR WEIGHT PROTEIN IN NON-MUSCLE CELLS
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DOI：
10.1016/0022-2836(77)90166-8
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发表时间：
1977-01-01
影响因子：
5.6
通讯作者：
LINDBERG, U
中科院分区：
文献类型：
--
作者：
CARLSSON, L;NYSTROM, LE;LINDBERG, U
小牛脾脏的复合物，含有肌动蛋白和一个较小的蛋白质称为profilin，以前分离。该复合物的一些特性进行了描述，它表明，与profilin协会是足以解释的持续单体状态的一些肌动蛋白在脾脏提取物。脾脏肌动蛋白也会与骨骼肌肌动蛋白重组，形成一种不可聚合的复合物，类似于从脾脏中分离的复合物。Profilin并不局限于脾脏，而是存在于多种其他组织和组织培养的细胞系中。肌动蛋白与profilin在细胞中的可逆结合可能提供了一种储存单体肌动蛋白和控制微丝周转的机制。
A complex from calf spleen, containing actin and a smaller protein called profilin, was previously isolated. Some properties of this complex are described and it is shown that association with profilin is sufficient to explain the persistent monomeric state of some of the actin in spleen extracts. Spleen profilin will also recombine with skeletal muscle actin to form a non-polymerizable complex resembling that isolated from spleen. Profilin is not restricted to spleen, but is found in a variety of other tissues and tissue-cultured cell lines. Reversible association of actin with profilin in the cell may provide a mechanism for storage of monomeric actin and controlled turnover of microfilaments.