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 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.
CNRS ESA 6031, IBMIG Université de Poitiers, France.
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A
Ottavi
E
E
Tiennault
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A
Maftah
J M
JM
Berjeaud
Y
Y
Cenatiempo
R
R
Julien
D001483:Base Sequence; D002846:Chromatography, Affinity; D003001:Cloning, Molecular / Q000379:methods; D017931:DNA Primers; D004926:Escherichia coli; D015951:Factor Xa; D016133:Polymerase Chain Reaction; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis; D014660:Vasoactive Intestinal Peptide / Q000031:analogs & derivatives* / Q000096:biosynthesis* / Q000302:isolation & purification
D017931:DNA Primers; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D014660:Vasoactive Intestinal Peptide; D015951:Factor Xa