An improved method to obtain a single recombinant vasoactive intestinal peptide (VIP) analog

The vasoactive intestinal peptide (VIP) is an ubiquitous peptide of great potential for applications. Development of new bioactive VIP analogs using production in recombinant E coli has been carried out in our laboratory. This work presents a new multimeric fusion protein expressing several VIP unit...

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Bibliographic Details
Published in:Biochimie 1998-04, Vol.80 (4), p.289-293
Main Authors: Ottavi, A., Tiennault, E., Maftah, A., Berjeaud, J.M., Cenatiempo, Y., Julien, R.
Format: Article
Language:English
Subjects:
Base Sequence
Chromatography, Affinity
Cloning, Molecular - methods
concatemer
DNA Primers
Escherichia coli
Factor Xa
Life Sciences
Polymerase Chain Reaction
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - isolation & purification
recombinant peptides
Recombinant Proteins - biosynthesis
Vasoactive Intestinal Peptide - analogs & derivatives
Vasoactive Intestinal Peptide - biosynthesis
Vasoactive Intestinal Peptide - isolation & purification
VIP analogs
Citations: Items that this one cites
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Description
Summary:The vasoactive intestinal peptide (VIP) is an ubiquitous peptide of great potential for applications. Development of new bioactive VIP analogs using production in recombinant E coli has been carried out in our laboratory. This work presents a new multimeric fusion protein expressing several VIP units separated by factor Xa cleavage site linkers. The steps leading from the affinity purification of the fusion protein and its processing by the factor Xa to the full characterization of the new bioactive improved VIP analog are also described.
ISSN:0300-9084
1638-6183
DOI:10.1016/S0300-9084(98)80069-2