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Purification and amino acid sequence of vasoactive intestinal peptide, peptide histidine isoleucinamide (1-27) and secretin from the small intestine of guinea pig

par Buscail, Louis ;Cauvin, Annick ;Gourlet, Philippe ;Gossen, Denis ;De Neef, Philippe ;Rathe, Jean ;Robberecht, Patrick ;Vandermeers-Piret, Marie-Claire ;Vandermeers, André ;Christophe, Jean
Référence Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1038, 3, page (355-359)
Publication Publié, 1990

Article révisé par les pairs

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Résumé :

The neuropeptides vasoactive intestinal peptide (VIP) and peptide histidine isoleucinamide (1-27) (PHI) and the hormone secretin were purified from the small intestine of guinea pig, being detected by radioimmunoassay and radioreceptor assay throughout six to seven chromatographic steps. After elution on a reverse-phase C18 column, the three peptides were separated on a Fractogel column. After cation-exchange chromatography of each peptide on Mono S, the final steps were performed using a reverse-phase RP8-e column. Guinea pig PHI differed from porcine PHI in having Tyr and Arg residues instead of Phe and Lys in, respectively, position 10 and 20. We confirmed the original sequence of guinea pig VIP previously documented (with Leu5, Thr9, Met19 and Val26). We also established the similarity of the primary structure of guinea pig secretin with that of porcine and bovine.