| 在大肠杆菌内高效表达大分子量拟蜘蛛牵丝蛋白 |
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| 引用本文： | 许红韬,樊宝良,曹更生,胡晓湘,李宁.在大肠杆菌内高效表达大分子量拟蜘蛛牵丝蛋白[J].农业生物技术学报,2006,14(4):522-525. |
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| 作者姓名： | 许红韬 樊宝良 曹更生 胡晓湘 李宁 |
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| 作者单位： | 中国农业大学农业生物技术国家重点实验室,北京,100094 |
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| 基金项目： | 国家高技术研究发展计划(863计划);北京市自然科学基金 |
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| 摘 要： | 依据已报道的蜘蛛(Nephilaclavipes)牵丝蛋白部分cDNA序列,设计合成两种不同结构的拟蜘蛛牵丝蛋白基因单体,大小分别为360和390bp。多聚化得到8倍体和16倍体后,克隆到表达载体pET-30a,得到4种表达载体,转化大肠杆菌(Escherichiacoli)BL21(DE3)诱导表达。用自制的抗蜘蛛牵丝蛋白血清Westernblot检测,表达产物呈梯度排列,主带与预计大小一致。蜘蛛牵丝蛋白表达量最高为800mg/L。
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| 关 键 词： | 蜘蛛 牵丝蛋白 大肠杆菌 表达 |
| 文章编号： | 1006-1304（2006）04-0522-04 |
| 收稿时间： | 2005-03-24 |
| 修稿时间： | 2006-06-21 |
Expression of High-molecular-weight Artificial Spider Dragline Silk Protein in Escherichia coli |
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| XU Hong-tao,FAN Bao-liang,CAO Geng-sheng,HU Xiao-xiang,LI Ning.Expression of High-molecular-weight Artificial Spider Dragline Silk Protein in Escherichia coli[J].Journal of Agricultural Biotechnology,2006,14(4):522-525. |
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| Authors: | XU Hong-tao FAN Bao-liang CAO Geng-sheng HU Xiao-xiang LI Ning |
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| Institution: | State Key Laboratory for Agrobiotechnology, China Agriculture University, Beijing 100094, China |
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| Abstract: | According to the known partial cDNA sequence of dragline silk, two artificial dragline silk gene monomers, 360 and 390 bp sequences, were designed to encode analogs of the protein of Nephila clavipes dragline silk. DNA monomer sequence was multimerized to encode high weight artificial spider dragline silk protein. Eight-timer and sixteen-timer were cloned into pET-30a vector and produced four-expression vector. Four-expression vectors were expressed in Escherichia coli respectively and produced a characteristic heterogeneous array of immunoreactive bands. The masses of the strongest band were respectively 85, 165, 85 and 165 kD, which represented the full-length gene product in each pattern. The highest concentration of recombinant dragline silk protein was 800 mg/L. |
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| Keywords: | spider (Nephila clavipes) dragline silk protein Escherichia coli expression |
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