Further purification of a polypeptide demonstrating enterogastrone activity
Open Access
- 1 July 1970
- journal article
- research article
- Published by Wiley in The Journal of Physiology
- Vol. 209 (1) , 57-64
- https://doi.org/10.1113/jphysiol.1970.sp009155
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.Keywords
This publication has 4 references indexed in Scilit:
- Preparation of highly active enterogastroneCanadian Journal of Physiology and Pharmacology, 1969
- The electrophoresis of histones in polyacrylamide gel and their quantitative determinationBiochemical Journal, 1967
- The Gastrointestinal Hormones, Secretin and Cholecystokinin-PancreozyminAnnals of Internal Medicine, 1961
- Two-dimensional paper chromatographic systems with high resolving power for amino acidsBiochimica et Biophysica Acta, 1953