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.

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