THE PURIFICATION OF 125I-GLUCAGON OF HIGH SPECIFIC ACTIVITY FOR RADIOIMMUNOCHEMICAL ESTIMATION OF GLUCAGON AND A QUALITATIVE COMPARISON OF GLUCAGON FROM DIFFERENT SOURCES

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Abstract
Radioactively labelled glucagon gave a low percentage binding with antibodies. This was not caused by a low antibody concentration in the antisera, but due to lack of reactivity of a part of the labelled glucagon to the antibodies. The radioactive glucagon was purified therefore by antibody binding and isolation of the antigen-antibody complex by gelfiltration. 125I-glucagon suitable for radioimmunochemical assay was obtained after dissociation of the complex. Parallelism of response was studied in beef-pork glucagon, pork glucagon, extracts of dog and human pancreas and extracts of human plasma. From the results it was concluded that the antiglucagon serum used did not discriminate between beef-pork, pork, human and dog glucagon. Moreover glucagon was identified radioimmunochemically in extracts of some parts of the human gastrointestinal tract.