PURIFICATION AND CHARACTERIZATION OF RECOMBINANT SPIDER SILK EXPRESSED IN ESCHERICHIA-COLI

Authors
ARCIDIACONO S MELLO C KAPLAN D CHELEY S BAYLEY H
Citation
S. Arcidiacono et al., PURIFICATION AND CHARACTERIZATION OF RECOMBINANT SPIDER SILK EXPRESSED IN ESCHERICHIA-COLI, Applied microbiology and biotechnology, 49(1), 1998, pp. 31-38
Citations number
32
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Applied microbiology and biotechnology → ACNP
ISSN journal
01757598
Volume
49
Issue
1
Year of publication
1998
Pages
31 - 38
Database
ISI
SICI code
0175-7598(1998)49:1<31:PACORS>2.0.ZU;2-A
Abstract
A partial cDNA clone, from the 3' end of the dragline silk gene was is olated from Nephila clavipes major ampullate glands. This clone contai ns 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 fragme nt was cloned into Escherichia coli and a 43-kDa recombinant silk prot ein was expressed. Characterization of the purified protein by Western blot, amino acid composition analysis, and matrix-assisted laser deso rption ionization/time-of-flight mass spectrometry confirms it to be s pider dragline silk.