摘要
本文报道了全化学合成虎纹捕鸟蛛毒素－Ⅰ基因在大肠杆菌中的表达，表达产物为Ｎ－端是谷胱甘肽硫转移酶的融合蛋白．经ＧＳＨ－Ｓｅｐｈａｒｏｓｅ４Ｂ亲和层析纯化，凝血酶酶解融合蛋白，得到重组ＨＷＴＸ－Ⅰ（ｒＨＷＴＸ－Ⅰ）．质谱和氨基酸顺序分析均表明ｒＨＷＴＸ－Ⅰ系正确表达产物．还原复性的ｒＨＷＴＸ－Ⅰ表现出与天然ＨＷＴＸ－Ⅰ生物学活性的一致性．
The chemical synthetic HWTX I gene was expressed in E.coli as a hybrid protein fused with glutathione S transferase(GST) at N terminal. The fusion protein was purified by GSH Sepharose 4B affinity column chromatography,and was cleaved by thrombin to obtain the recombinant HWTX I (rHWTX I).Mass spectrometry and amino acid sequence analysis proved that rHWTX I was expressed correctly.Renatured rHWTX I showed the same biological property with that of the native HWTX I.
出处
《生命科学研究》
CAS
CSCD
1998年第3期229-232,共4页
Life Science Research
基金
国家自然科学基金
国家"863"课题
关键词
蜘蛛
化学合成
原核表达
HWTX-Ⅰ基因
spider, Huwentoxin I gene, chemical synthesis, prokaryotic expression
