The mechanism of action of colchicine. Colchicine binding to sea urchin eggs and the mitotic apparatus.
The mechanism of action of colchicine. Colchicine binding to sea urchin eggs and the mitotic apparatus.
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秋水仙碱作用机理。秋水仙碱与海胆卵和有丝分裂设备结合。
DOI：
10.1083/jcb.34.2.535
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发表时间：
1967-08
影响因子：
7.8
通讯作者：
Taylor, E W
中科院分区：
文献类型：
--
作者：
Borisy, G G;Taylor, E W
秋水仙碱在体内与受精或未受精的海胆卵中存在的蛋白质形成复合物;在体外与来自卵匀浆的可溶性部分获得类似的结合。动力学参数和结合平衡常数在体内和体外基本相同。通过区域离心，显示结合位点蛋白具有6S的沉降常数。该蛋白质存在于分离的有丝分裂器的提取物中，其浓度比全卵匀浆中的浓度高数倍。在导致微管消失的条件下，在低离子强度下从有丝分裂器中提取。未检测到与Kane先前描述的27 S蛋白的结合，27 S蛋白是分离的有丝分裂器的主要蛋白组分。秋水仙素结合蛋白G的性质（结合常数，沉降常数，Sephadex洗脱体积）与从哺乳动物细胞，海胆精子尾和脑组织中获得的蛋白质相似，因此支持该蛋白质是微管亚基的结论。
Colchicine forms a complex in vivo with a protein present in fertilized or unfertilized sea urchin eggs; similar binding was obtained in vitro with the soluble fraction from egg homogenates. Kinetic parameters and binding equilibrium constant were essentially the same in vivo and in vitro. The binding site protein was shown to have a sedimentation constant of 6S by zone centrifugation. The protein was present in extracts of the isolated mitotic apparatus at a concentration which was several times higher than in whole-egg homogenates. It was extracted from the mitotic apparatus at low ionic strength under conditions which lead to the disappearance of microtubules. No binding could be detected to the 27S protein, previously described by Kane, which is a major protein component of the isolated mitotic apparatus. The properties of the colchicine-bindinG protein, (binding constant, sedimentation constant, Sephadex elution volume) are similar to those obtained with the protein from mammalian cells, sea-urchin sperm tails, and brain tissue, and thus support the conclusion that the protein is a subunit of microtubules.