Novel actin depolymerizing macrolide aplyronine A.
Novel actin depolymerizing macrolide aplyronine A.
复制标题
新型肌动蛋白解聚大环内酯 aplyronine A.
DOI：
--
复制
发表时间：
1996
期刊：
影响因子：
--
通讯作者：
H. Karaki
中科院分区：
文献类型：
--
作者：
S. Saito;S. Watabe;H. Ozaki;H. Kigoshi;Kiyoyuki Yamada;N. Fusetani;H. Karaki
Aaproronine A是从Aaprosia kurodai中分离的大环内酯。通过检测芘基肌动蛋白的荧光强度，发现阿克罗宁A抑制了肌动蛋白聚合的速度和程度。Aeacronine A也能迅速解聚F-肌动蛋白。解聚的动力学表明，阿克罗宁A切断F-肌动蛋白。在不同浓度的阿曲洛宁A下，总肌动蛋白和F-肌动蛋白的浓度之间的关系表明阿曲洛宁A与G-肌动蛋白形成1：1的复合物。从这些结果，可以得出结论，阿罗宁A抑制肌动蛋白聚合和解聚F-肌动蛋白的蚕食。比较aacronine A和另一种肌动蛋白解聚大环内酯，mycalcohol B的化学结构，表明aacronine A的侧链而不是大环内酯环可能是其肌动蛋白结合和切断活性的原因。
Aplyronine A is a macrolide isolated from Aplysia kurodai. By monitoring fluorescent intensity of pyrenyl-actin, it was found that aplyronine A inhibited both the velocity and the degree of actin polymerization. Aplyronine A also quickly depolymerized F-actin. The kinetics of depolymerization suggest that aplyronine A severs F-actin. The relationship between the concentration of total actin and F-actin at different concentrations of aplyronine A suggests that aplyronine A forms a 1:1 complex with G-actin. From these results, it is concluded that aplyronine A inhibits actin polymerization and depolymerizes F-actin by nibbling. Comparison of the chemical structure of aplyronine A and another actin-depolymerizing macrolide, mycalolide B, suggests that the side-chain but not the macrolide ring of aplyronine A may account for its actin binding and severing activity.
影响因子：
2.9
作者：
SAMPATH, P;POLLARD, TD
通讯作者：
POLLARD, TD
在 Ca2+ 存在下，原肌球蛋白对凝溶胶蛋白切断的肌动蛋白片段进行退火。
DOI：
--
发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ishikawa,R;Yamashiro,S;Matsumura,F
通讯作者：
Matsumura,F