Appl Environ Microbiol. 1996 May;62(5):1544-9. doi: 10.1128/aem.62.5.1544-1549.1996.
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.
采用(sup125)I 标记的激活毒素和从小菜蛾幼虫中肠分离的刷状缘膜泡,在体外对 Cry1Aa、Cry1Ac 和 Cry1Ba 毒素之间的结合和竞争进行了定量分析。三种毒素特异性结合到中肠刷状缘膜泡上。直接结合实验表明,Cry1Aa 和 Cry1Ba 识别具有不同亲和力的单一结合位点,而 Cry1Aa 识别两个结合位点,一个具有高亲和力和低浓度,另一个具有较低亲和力但较高浓度。竞争实验表明,Cry1Ac 和 Cry1Ba 毒素在小菜蛾中肠膜上共享一个结合位点,该位点也是 Cry1Aa 的低亲和力结合位点。