Interaction of arenastatin A with porcine brain tubulin.
Interaction of arenastatin A with porcine brain tubulin.
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阿那他汀 A 与猪脑微管蛋白的相互作用。
DOI：
10.1248/bpb.20.171
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发表时间：
1997
影响因子：
2
通讯作者：
S. Iwasaki
中科院分区：
文献类型：
--
作者：
K. Morita;Y. Koiso;Y. Hashimoto;M. Kobayashi;W. Wang;N. Ohyabu;S. Iwasaki
Arenastatin A是从冲绳海绵Dyside a arenaria中分离得到的一种含16元环的抗有丝分裂脱脂肽。用[~3H]阿司他丁A和其他微管阻断剂研究了该化合物与微管蛋白的相互作用。Scatchard分析表明，每个微管蛋白异源二聚体存在一个Arenastatin A结合位点，解离常数(Kd)为1.8×10(-6)M。根霉毒素是Arenastatin A结合的竞争性抑制剂，长春花碱也以部分竞争性的方式抑制Arenastatin A的结合。阿司他丁A对秋水仙碱与微管蛋白的结合无抑制作用。
Arenastatin A, isolated from the Okinawan marine sponge Dysidea arenaria, is an antimitotic depsipeptide containing a 16-membered ring. Interaction of the compound with tubulin was investigated by the use of [3H]arenastatin A and other microtubule disruptors. Scatchard analysis indicated the presence of one binding site for arenastatin A per tubulin heterodimer with a dissociation constant (Kd) of 1.8 x 10(-6) M. Rhizoxin was a competitive inhibitor of arenastatin A binding, and vinblastine also inhibited arenastatin A binding in a partially competitive manner. Arenastatin A had no inhibitory effect on colchicine binding to tubulin.