Abstract
Abstract Synthesis of porcine motilin is described. Construction of the entire molecule of this hormone was carried out by the fragment condensation method in solution employing Rudinger’s azide modification, and the resulting protected docosapeptide was deblocked by sodium–liquid ammonia procedure. Purification of the final product was performed by ion exchange chromatography on CM-Sephadex using ammonium acetate as eluent and gel filtration on BiO–Gel P-6. Purity of the synthetic docosapeptide was assessed by TLC in two different solvent systems and amino acid analysis. This polypeptide showed gastric motoractivity stimulating action on 30 min intravenous infusion in dogs in 5 ng/kg/min doses, which is characteristic to porcine motilin.
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