Abstract
The docosapeptide corresponding to the entire amino acid sequence of canine motilin, a newly characterized gastric motor activity-stimulating polypeptide, was synthesized by the conventional solution method. All protecting groups employed were removed by 1 M trifluoromethanesulfonic acid-thioanisole-trifluoroacetic acid and the deprotected peptide was purified by gel-filtration on Sephadex G-25, followed by partition chromatography and reverse phase high performance liquid chromatography. When contractile activity on rabbit duodenal muscle was examined, synthetic canine motilin was as active as synthetic porcine motilin. The relative potencies of Lys1 and Ser1 derivatives prepared in the same manner as canine motilin were ca. 1/1000 and 1/250, respectively.
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