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A human minigastrin-II analog was prepared by conventional methods in solution using N-benzyloxycarbonyltyrosine O-sulfate as starting material in the synthetic route. Upon removal of the acid-labile protecting groups and purification by preparative reversed-phase chromatography the sulfated gastrin peptide was obtained in satisfactory overall yields as homogeneous material. It was found to be about twice as active as the non-sulfated form in stimulating gastric acid secretion and to exhibit a 10-fold higher affinity to gastrin receptors of purified parietal cells.
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