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When plasma from human or rats with or without hepatic injury was filtrated by columns of Bio Gel P-30, P-150 and P-300, "big plasma glucagon" (BPG), a large molecular weight form of immunoreactive glucagon (IRG), was always eluted together with glucagon degrading activity (GDA) at the void volume. The GDA in BPG fraction obtained by gel filtration from normal rats was suppressed mainly by serine and thiol proteinase inhibitors and that from carbon tetrachloride (CCl4)-treated rats was suppressed by thiol proteinase inhibitors. The IRG values in BPG fraction decreased in parallel with inhibition of the GDA. The GDA in BPG fraction obtained by a column of Bio Gel A-1.5m from plasma both normal and CCl4-treated rats was strongly inhibited by p-chloromercuriphenyl sulfonate and N-ethylmaleimide, and IRG values in BPG fraction also decreased to near zero by addition of those inhibitors to the assay system. The GDA and IRG in BPG fraction in human plasma from normal subjects and cirrhotic patients showed almost the same chromatographic profiles as those obtained from rats. These results indicate that IRG in BPG fraction in plasma from human and rats could be apparent values accounted for the degradation of 125I-labeled glucagon by plasma proteinases during the assay procedure.
財団法人日本消化器病学会の論文