Heterogeneity of extractable gut glucagon-like immunoreactivity (GLI) and its lipolytic activity

Gut glucagon-like immunoreactivity (GLI) was extracted from the mucosa of the canine intestine and was separated into two peaks by gel filtration; Peak I (7,000 daltons) and Peak II (3,500 daltons). These two peaks were purified by means of affinity chromatography using an anti-glucagon antibody as a ligand substance. These purified gut GLIs were not composed of single component, when applied to ion exchange chromatography. These partially purified Peak I and Peak II showed lipolytic activities, though very weak in potency, in vitro on the rat fat tissue at pharmacologically high concentration (5 ng eq/ml in final). It was concluded that gut GLI, even though purified, showed heterogeneity and that gut GLI revealed lipolytic activity although weak in potency compared with pancreatic glucagon.