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[微管蛋白聚合的体外研究。ATP、长春碱和异沙诺宁的作用(作者译)]

[In vitro study of tubulin polymerisation. Effects of ATP, vinblastine and isaxonine (author's transl)].

作者信息

Coelho R, Istin M

出版信息

Nouv Presse Med. 1982 Apr 8;11(16):1227-32.

PMID:6896570
Abstract

The dual action of vinblastine on tubulin, namely disruption and aggregation, is analyzed by turbidimetry. The existence of two different binding sites for the alkaloid is confirmed. The high affinity site binds vinblastine at low concentrations, at which no effect is observed on depolymerized tubulin, but where pre-formed microtubules are disrupted. The low affinity site is associated with tubulin aggregation. The binding constants of these two sites have been evaluated. Isaxonine (N-isopropyl-amino-2 pyrimidine) partially inhibits the effects of vinblastine, both on microtubule disruption and tubulin aggregation.

摘要

通过比浊法分析了长春碱对微管蛋白的双重作用,即破坏和聚集。证实了该生物碱存在两个不同的结合位点。高亲和力位点在低浓度下结合长春碱,此时对解聚的微管蛋白没有影响,但预先形成的微管会被破坏。低亲和力位点与微管蛋白聚集有关。已评估了这两个位点的结合常数。异长春碱(N-异丙基-氨基-2-嘧啶)部分抑制长春碱对微管破坏和微管蛋白聚集的作用。

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