Abstract

Natural porcine secretin was purified by high performance liquid chromatography (HPLC) in order to compare it with synthetic secretin. As a starting material we used partially purified secretin obtained by extraction from porcine duodenum followed by purification by ion-exchange chromatography and gel filtration. Preparative HPLC was performed on a reverse-phase column with a volatile eluent. The biological activity of the purified secretin was 5450 c.u./mg in the anesthetized rat, which is higher than those of other natural secretins reported so far (4000 c.u./mg), and was reasonably close to that of our synthetic secretin (5750 c.u./mg). The natural and synthetic secretins were compared by several physicochemical methods.

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