Abstract
The 36-residue sequence of human pancreatic polypeptide (HPP) was synthesized by solid-phase methodology, cleaved from the benzhydrylamine resin by HF treatment, and purified by gel filtration, ion exchange, and partition chromatography. In addition to the usual criteria, the homogeneity of the final product was examined by reversed phase high performance liquid chromatography. This technique was also used to isolate and characterize the cyanogen bromide cleavage fragments, and finally to compare the synthetic product with native human, bovine, and porcine pancreatic polypeptide isolated from natural sources. The purified HPP, like native PP, was a potent inhibitor of pancreatic secretion in the dog.
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