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. 1970 Jul;209(1):57-64.
doi: 10.1113/jphysiol.1970.sp009155.

Further purification of a polypeptide demonstrating enterogastrone activity

Further purification of a polypeptide demonstrating enterogastrone activity

J C Brown et al. J Physiol. 1970 Jul.

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 mug/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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References

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    1. Biochim Biophys Acta. 1953 Feb;10(2):344-5 - PubMed
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