Purification and characterization of recombinant spider silk expressed in Escherichia coli |
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| Authors: | S. Arcidiacono C. Mello D. Kaplan S. Cheley H. Bayley |
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| Affiliation: | (1) Biotechnology Division, U.S. Army Natick Army Research, Development, and Engineering Center, Natick, MA 01760, USA Tel.: +1 (508) 233 5513; Fax: +1 (508) 233 5521, US;(2) Tufts University, Medford, MA 02155, USA, US;(3) Texas A&M University, College station, TX 77843, USA, US |
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| 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 desorption ionization/time-of-flight mass spectrometry confirms it to be spider dragline silk. Received: 7 April 1997 / Received revision: 24 July 1997 / Accepted: 25 August 1997 |
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