Purification and characterization of recombinant spider silk expressed in Escherichia coli
- Cite this article as:
- Arcidiacono, S., Mello, C., Kaplan, D. et al. Appl Microbiol Biotechnol (1998) 49: 31. doi:10.1007/s002530051133
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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.