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- W2101367047 abstract "Research Article1 October 1986free access Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins. U. Eisel U. Eisel Search for more papers by this author W. Jarausch W. Jarausch Search for more papers by this author K. Goretzki K. Goretzki Search for more papers by this author A. Henschen A. Henschen Search for more papers by this author J. Engels J. Engels Search for more papers by this author U. Weller U. Weller Search for more papers by this author M. Hudel M. Hudel Search for more papers by this author E. Habermann E. Habermann Search for more papers by this author H. Niemann H. Niemann Search for more papers by this author U. Eisel U. Eisel Search for more papers by this author W. Jarausch W. Jarausch Search for more papers by this author K. Goretzki K. Goretzki Search for more papers by this author A. Henschen A. Henschen Search for more papers by this author J. Engels J. Engels Search for more papers by this author U. Weller U. Weller Search for more papers by this author M. Hudel M. Hudel Search for more papers by this author E. Habermann E. Habermann Search for more papers by this author H. Niemann H. Niemann Search for more papers by this author Author Information U. Eisel, W. Jarausch, K. Goretzki, A. Henschen, J. Engels, U. Weller, M. Hudel, E. Habermann and H. Niemann The EMBO Journal (1986)5:2495-2502https://doi.org/10.1002/j.1460-2075.1986.tb04527.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info A pool of synthetic oligonucleotides was used to identify the gene encoding tetanus toxin on a 75-kbp plasmid from a toxigenic non-sporulating strain of Clostridium tetani. The nucleotide sequence contained a single open reading frame coding for 1315 amino acids corresponding to a polypeptide with a mol. wt of 150,700. In the mature toxin molecule, proline (2) and serine (458) formed the N termini of the 52,288 mol. wt light chain and the 98,300 mol. wt heavy chain, respectively. Cysteine (467) was involved in the disulfide linkage between the two subchains. The amino acid sequences of the tetanus toxin revealed striking homologies with the partial amino acid sequences of botulinum toxins A, B, and E, indicating that the neurotoxins from C. tetani and C. botulinum are derived from a common ancestral gene. Overlapping peptides together covering the entire tetanus toxin molecule were synthesized in Escherichia coli and identified by monoclonal antibodies. The promoter of the toxin gene was localized in a region extending 322 bp upstream from the ATG codon and was shown to be functional in E. coli. Previous ArticleNext Article Volume 5Issue 101 October 1986In this issue RelatedDetailsLoading ..." @default.
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- W2101367047 title "Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins." @default.
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