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

Ottavi, A; Tiennault, E; Maftah, A; Berjeaud, J M; Cenatiempo, Y; Julien, R

Ottavi, A; Tiennault, E; Maftah, A; Berjeaud, J M; Cenatiempo, Y; Julien, R.

Affiliation

Ottavi A; CNRS ESA 6031, IBMIG Université de Poitiers, France.

Biochimie ; 80(4): 289-93, 1998 Apr.

Article in En | MEDLINE | ID: mdl-9672747

ABSTRACT

ABSTRACT

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.

Subject(s)

Vasoactive Intestinal Peptide/analogs & derivatives; Vasoactive Intestinal Peptide/biosynthesis; Base Sequence; Chromatography, Affinity; Cloning, Molecular/methods; DNA Primers; Escherichia coli; Factor Xa; Polymerase Chain Reaction; Recombinant Fusion Proteins/biosynthesis; Recombinant Fusion Proteins/isolation & purification; Recombinant Proteins/biosynthesis; Vasoactive Intestinal Peptide/isolation & purification

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Collection: 01-internacional Database: MEDLINE Main subject: Vasoactive Intestinal Peptide Language: En Journal: Biochimie Year: 1998 Document type: Article Affiliation country: France

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