IDENTIFICATION AND PARTIAL-PURIFICATION OF A BACILLUS-THURINGIENSIS CRYIC DELTA-ENDOTOXIN BINDING-PROTEIN FROM SPODOPTERA-LITTORALIS GUT MEMBRANES
IDENTIFICATION AND PARTIAL-PURIFICATION OF A BACILLUS-THURINGIENSIS CRYIC DELTA-ENDOTOXIN BINDING-PROTEIN FROM SPODOPTERA-LITTORALIS GUT MEMBRANES
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DOI：
10.1016/0014-5793(93)81305-j
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发表时间：
1993-02-01
期刊：
影响因子：
3.5
通讯作者：
ELLAR, DJ
中科院分区：
文献类型：
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作者：
SANCHIS, V;ELLAR, DJ
使用 CryIC 和 CryIA(c) 苏云金芽孢杆菌 δ-内毒素进行免疫印迹实验，以检测斜纹夜蛾刷状缘膜囊泡上是否存在特异性毒素结合蛋白。 CryIC 毒素结合 40 和 65 kDa 的两种蛋白质，CryIA(c) 结合 40 kDa 的蛋白质。 CryIA(c) 毒素还与北沙蚕刷状缘膜囊泡上的 120 kDa 蛋白微弱结合，针对来自 Manduca sexta 的推定 CryIA(c) 120 kDa 结合蛋白产生的多克隆抗血清也是如此。 40 kDa CryIC 结合蛋白通过亲和层析进行部分纯化，因此是体内北沙门氏菌 CryIC 毒素受体的有力候选者。
Immunoblotting experiments were performed using CryIC and CryIA(c) Bacillus thuringiensis delta-endotoxins to detect the presence of specific toxin binding proteins on Spodoptera littoralis brush border membrane vesicles. The CryIC toxin binds two proteins of 40 and 65 kDa and the CryIA(c) binds a protein of 40 kDa. The CryIA(c) toxin also binds faintly to a 120 kDa protein on S. littoralis brush border membrane vesicles as does a polyclonal antiserum raised against a putative CryIA(c) 120 kDa binding protein from Manduca sexta. The 40 kDa CryIC binding protein was partially purified by affinity chromatography and is therefore a strong candidate for in vivo S. littoralis CryIC toxin receptor.