Purification and characterization of recombinant spider silk expressed in Escherichia coli
Purification and characterization of recombinant spider silk expressed in Escherichia coli
复制标题
DOI：
10.1007/s002530051133
复制
发表时间：
1998-01-01
影响因子：
5
通讯作者：
Bayley, H
中科院分区：
文献类型：
--
作者：
Arcidiacono, S;Mello, C;Bayley, H
A partial cDNA clone, from the 3' end of the dragline silk gene was isolated from Nephila clavipes major ampullate glands. This clone contains a 1.7-kb insert, consisting of a repetitive coding region of 1.4-kb and a 0.3-kb nonrepetitive coding region; 1.5-kb of the 1.7-kb fragment was cloned into Escherichia coli and a 43-kDa recombinant silk protein was expressed. Characterization of the purified protein by Western blot, amino acid composition analysis, and matrix-assisted laser desorption ionization/time-of-flight mass spectrometry confirms it to be spider dragline silk.
