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Appl Microbiol Biotechnol. 1998 Jan;49(1):31-8.

Purification and characterization of recombinant spider silk expressed in Escherichia coli.

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Biotechnology Division, U.S. Army Natick Army Research, Development, and Engineering Center, Natick, MA 01760, USA.


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.

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