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| Expression of High-molecular-weight Artificial Spider Dragline Silk Protein in Escherichia coli |
| XUHong-tao;FANBao-liang;CAOGeng-sheng;HUXiao-xiang;LINing |
| 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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Received: 30 March 2005
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