Glycoprotein-like Large Glucagon Immunoreactive Species in Extracts of the Fetal Bovine Pancreas

Large glucagon immunoreactive substances, extracted from the fetal bovine pancreas and separated by gel filtration in the presence of 6 M guanidiniumhydrochloride, were submitted to lectin-sepharose affinity column chromatography. Gel-filtered peak I (∼45 KΔ) and peak II (∼10 Δ) interacted biospecifically with concanavalin-A- and wheat-germ-lectin-sepharoses, suggesting glycoproteins as possible constituents of large glucagon immunoreactive substances in extracts of the fetal bovine pancreas. The glucagon-like immunochemical identity of the lectinsepharose-bound substances was further substantiated by binding to antiglucagon antibodies-sepharose and by characteristic proportional dilutions in the glucagon radioimmunoassay.