Further purification of a polypeptide demonstrating enterogastrone activity

Abstract

1. The further purification of a polypeptide having potent enterogastrone activity, without CCK—PZ effects, is described. 2. The material was inhibitory when doses of 1·0 μg/kg.hr were administered intravenously. Amino acid analyses demonstrated the absence of proline, a high content of glutamine and a preponderance of lysine over arginine. Tryptic degradation destroys the inhibitory effect of the polypeptide. Further studies must be performed before the physiological status of the polypeptide can be ascertained.