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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.

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