BINDING OF MAYTANSINE TO RAT-BRAIN TUBULIN
BINDING OF MAYTANSINE TO RAT-BRAIN TUBULIN
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DOI：
10.1016/0006-291x(76)90958-x
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发表时间：
1976-01-01
影响因子：
3.1
通讯作者：
JOHNS, DG
中科院分区：
文献类型：
--
作者：
MANDELBAUMSHAVIT, F;WOLPERTDEFILIPPES, MK;JOHNS, DG
美坦辛和长春新碱与粗大鼠脑微管蛋白的结合是一个依赖温度和离子强度的过程。长春新碱和美坦辛结合的Ka值为0.5倍。106M-1和1.5倍。106M-1。美坦辛竞争性地抑制长春新碱与KI的结合。美坦辛为0.4倍。10-6M。两种抗癌药物的结合是可逆的。未标记的美坦辛迅速取代了标记的药物；只有大约75%的结合的美坦辛被长春新碱取代。标记长春新碱的结合完全被长春新碱或美坦辛取代。这两种药物似乎共享一个共同的结合位点，尽管似乎存在一个额外的梅坦辛特异结合位点。秋水仙碱不影响长春新碱或美坦辛的结合。
Maytansine and vincristine binding to crude rat brain tubulin is a temperature- and ionic strength dependent process. The Ka values for binding of vincristine and maytansine are 0.5 .times. 106 M-1 and 1.5 .times. 106 M-1, respectively. Maytansine competitively inhibits vincristine binding with a Ki. for maytansine of 0.4 .times. 10-6 M. The binding of both antitumor drugs is easily reversible. Unlabeled maytansine rapidly displaces the labeled drug; only about 75% of bound maytansine was displaced by vincristine. Bound labeled vincristine is completely displaced by vincristine or maytansine. Both drugs appear to share a common binding site, although an additional site specific for maytansine seems to be present. Colchicine did not affect vincristine or maytansine binding.