Skip to main content
The Journal of Physiology logoLink to The Journal of Physiology
. 1970 Jul;209(1):57–64. doi: 10.1113/jphysiol.1970.sp009155

Further purification of a polypeptide demonstrating enterogastrone activity

J C Brown, V Mutt, R A Pederson
PMCID: PMC1396039  PMID: 5499047

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.

Full text

PDF
57

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brown J. C., Pederson R. A., Jorpes E., Mutt V. Preparation of highly active enterogastrone. Can J Physiol Pharmacol. 1969 Jan;47(1):113–114. doi: 10.1139/y69-020. [DOI] [PubMed] [Google Scholar]
  2. JORPES J. E., MUTT V. The gastrointestinal hormones, secretin and cholecystokinin-pancreozymin. Ann Intern Med. 1961 Sep;55:395–405. doi: 10.7326/0003-4819-55-3-395. [DOI] [PubMed] [Google Scholar]
  3. Johns E. W. The electrophoresis of histones in polyacrylamide gel and their quantitative determination. Biochem J. 1967 Jul;104(1):78–82. doi: 10.1042/bj1040078. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. REDFIELD R. R. Two-dimensional paper chromatographic systems with high resolving power for amino acids. Biochim Biophys Acta. 1953 Feb;10(2):344–345. doi: 10.1016/0006-3002(53)90260-1. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Physiology are provided here courtesy of The Physiological Society

RESOURCES