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首页> 外文期刊>Applied and Environmental Microbiology >Binding of Bacillus thuringiensis Cry1 Toxins to the Midgut Brush Border Membrane Vesicles of Chilo suppressalis (Lepidoptera: Pyralidae): Evidence of Shared Binding Sites.
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Binding of Bacillus thuringiensis Cry1 Toxins to the Midgut Brush Border Membrane Vesicles of Chilo suppressalis (Lepidoptera: Pyralidae): Evidence of Shared Binding Sites.

机译:苏云金芽孢杆菌Cry1毒素绑定到中肠刷边界膜囊泡的suppress(鳞翅目:P科):共享结合位点的证据。

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摘要

Binding and competition among Cry1Aa, Cry1Ac, and Cry1Ba toxins were analyzed quantitatively in vitro by using (sup125)I-labeled activated toxins and brush border membrane vesicles isolated from Chilo suppressalis larval midguts. The three toxins bound specifically to the midgut brush border membrane vesicles. Direct binding experiments showed that Cry1Aa and Cry1Ba recognized a single class of binding sites with different affinities, whereas Cry1Aa recognized two classes of binding sites, one with a high affinity and a low concentration and the other with a lower affinity but higher concentration. Competition experiments showed that toxins Cry1Ac and Cry1Ba shared a binding site in the C. suppressalis midgut membranes and that this site was also the low-affinity binding site for Cry1Aa.
机译:通过使用(sup125)I标记的活化毒素和分离自Chilohibialis幼虫中肠的刷状缘膜囊泡对Cry1Aa,Cry1Ac和Cry1Ba毒素之间的结合和竞争进行了体外定量分析。这三种毒素特异结合于中肠刷状缘膜囊泡。直接结合实验表明,Cry1Aa和Cry1Ba识别具有不同亲和力的一类结合位点,而Cry1Aa识别两类结合位点,一类具有高亲和力和低浓度,另一类具有较低的亲和力和更高的浓度。竞争实验表明,毒素Cry1Ac和Cry1Ba在抑制杯中肠膜中共享一个结合位点,并且该位点也是Cry1Aa的低亲和力结合位点。

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