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Purification and amino acid sequence of vasoactive intestinal peptide, peptide histidine isoleucinamide and secretin from the ovine small intestine

par Bounjoua, Yassir;Vandermeers, André ;Robberecht, Patrick ;Vandermeers-Piret, Marie-Claire ;Christophe, Jean
Référence Regulatory peptides, 32, 2, page (169-179)
Publication Publié, 1991

Article révisé par les pairs

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Résumé :

Vasoactive intestinal peptide (VIP), peptide histidine isoleucinamide (PHI) and secretin were separated and purified to homogeneity from ovine small intestine, using radioimmunoassay and radioreceptor assay for detection. An efficient and rapid purification sequence included acid extraction, concentration on a bulk C18 cartridge, filtration on a Fractogel column, ion-exchange chromatography on Mono-S and a maximum of three successive reverse-phase HPLC steps. The amounts of peptides obtained from 450 g wet weight tissue were 20 μg VIP, 15 μg PHI and 5 μg secretin. The as yet unknown amino acid sequences of the three peptides were found to be identical to those of the corresponding bovine peptides.