电荷对微管蛋白秋水仙碱结合位点的影响。

Charge effect on the colchicine binding-site of tubulin.

作者信息

Roychowdhuri S, Banerjee A, Bhattacharyya B

出版信息

Biochem Biophys Res Commun. 1983 Jun 15;113(2):384-90. doi: 10.1016/0006-291x(83)91738-2.

Abstract

Poly(L-lysine) was found to enhance colchicine binding activity of brain tubulin to a several folds. Bases of biological interests that were tested and found to be inactive were spermine, spermidine and even L-lysine. Part of this enhance binding is due to the increase in the affinity of colchicine-tubulin interaction in the presence of poly(L-lysine). Moreover, poly(L-lysine) stabilized the colchicine binding site of tubulin against thermal denaturation.

摘要

发现聚（L-赖氨酸）可将脑微管蛋白的秋水仙碱结合活性提高数倍。经测试发现无活性的具有生物学意义的碱基有精胺、亚精胺，甚至L-赖氨酸。这种结合增强的部分原因是在聚（L-赖氨酸）存在的情况下秋水仙碱与微管蛋白相互作用的亲和力增加。此外，聚（L-赖氨酸）使微管蛋白的秋水仙碱结合位点对热变性稳定。