Purification and characterization of recombinant spider silk expressed in Escherichia coli
@article{Arcidiacono1998PurificationAC, title={Purification and characterization of recombinant spider silk expressed in Escherichia coli}, author={Steven Arcidiacono and Charlene M. Mello and Drora Kaplan and Stephen Cheley and Hagan Bayley}, journal={Applied Microbiology and Biotechnology}, year={1998}, volume={49}, pages={31-38} }
Abstract 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…
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