Physicochemical and biological properties of glucagon-like polypeptides from porcine colon

J. Michael Conlon, Richard F. Murphy, Keith D. Buchanan

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


Polypeptide material displaying glucagon-like immunoreactivity was isolated from porcine colon using immunoaffinity chromatography. The immunoreactive material was tightly bound to high molecular weight proteins but was dissociated by 0.1% w/v sodium dodecyl sulphate solution into immunoreactive components of approximate molecular weights 12 000, 8000, 5000 and 3000. These components reacted at least 50 times more strongly with antibodies specific for the N-terminal region of glucagon than with antibodies specific for the C-terminal region of glucagon. While the 8000 and 3000 dalton fractions were homogeneous, the 12 000 and 5000 dalton fractions were resolved into multiple bands by isoelectric focusing. The 12 000 dalton fraction was devoid of glycogenolytic and lipolytic activity, was not insulin releasing and showed no ability to bind to receptor sites specific for glucagon on hepatic plasma membranes and to active hepatic adenylate cyclase. The 8000 and 5000 dalton components showed weak lipolytic activity. The possible significance of colonic glucagon-like immunoreactivity relative to pancreatic glucagon and immunoreactivity from other tissues is discussed.

Original languageEnglish
Pages (from-to)229-240
Number of pages12
JournalBBA - Protein Structure
Issue number2
Publication statusPublished (in print/issue) - 25 Apr 1979


  • (Colon, Pancreas)
  • Glucagon-like polypeptide
  • Immunoreactivity


Dive into the research topics of 'Physicochemical and biological properties of glucagon-like polypeptides from porcine colon'. Together they form a unique fingerprint.

Cite this