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除草剂氟乐灵与衣藻鞭毛微管蛋白的结合。

Binding of the herbicide trifluralin to Chlamydomonas flagellar tubulin.

作者信息

Hess F D, Bayer D E

出版信息

J Cell Sci. 1977 Apr;24:351-60. doi: 10.1242/jcs.24.1.351.

DOI:10.1242/jcs.24.1.351
PMID:893549
Abstract

Colchicine-binding tubulin was isolated from the centre 2 axoneme microtubules from the flagella of the alga Chlamydomonas eugametos. Incubating this tubulin with 5-8 micron [14C]trifluralin resulted in significant and reproducible binding of trifluralin to tubulin. The specificity of binding was determined by demonstrating that limited or no binding occurred to flagellar membrane and matrix protein, higher plant proteins, or bovine serum albumin. It was concluded that trifluralin, at obtainable soluble concentrations, specifically inhibits microtubule-mediated processes in plants. To date no effect of trifluralin on animal microtubule systems has been reported; therefore, it is suggested that trifluralin has revealed a pharmacological difference between plant and animal tubulin.

摘要

秋水仙碱结合微管蛋白是从衣藻(Chlamydomonas eugametos)鞭毛的中心2轴丝微管中分离出来的。将这种微管蛋白与5-8微米的[14C]氟乐灵一起孵育,结果显示氟乐灵与微管蛋白发生了显著且可重复的结合。通过证明氟乐灵与鞭毛膜和基质蛋白、高等植物蛋白或牛血清白蛋白的结合有限或不发生,确定了结合的特异性。得出的结论是,在可获得的可溶性浓度下,氟乐灵特异性抑制植物中微管介导的过程。迄今为止,尚未报道氟乐灵对动物微管系统有影响;因此,有人认为氟乐灵揭示了植物和动物微管蛋白之间的药理学差异。

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