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Iodoglucagon. Preparation and characterization.

B Desbuquois

    European Journal of Biochemistry
    |May 6, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Iodinated glucagon derivatives show increased potency and receptor binding, with optimal effects at 3-4 iodine atoms. Monoiodination enhances glucagon

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    Area of Science:

    • Biochemistry
    • Endocrinology
    • Molecular Biology

    Background:

    • Glucagon is a key hormone regulating glucose metabolism.
    • Modifications to glucagon can alter its biological activity and receptor interactions.

    Purpose of the Study:

    • To synthesize and characterize iodinated glucagon derivatives.
    • To evaluate the impact of iodination on glucagon's biological potency, receptor binding, and metabolic stability.

    Main Methods:

    • Glucagon was reacted with iodine monochloride to create iodinated derivatives.
    • Iodoamino acid composition was analyzed using ion-exchange chromatography and electrophoresis.
    • Biological activity was assessed by measuring adenylate cyclase stimulation and receptor binding affinity.
    • In vitro inactivation by liver membranes and plasma was evaluated.

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    Main Results:

    • Iodination primarily occurs at tyrosyl residues (10 and 13) and secondarily at a histidyl residue.
    • Iodinated glucagons (1-4 iodine atoms) exhibit enhanced adenylate cyclase activity (up to 5-fold) and receptor binding (up to 2-fold).
    • Higher degrees of iodination (beyond 4 atoms) slightly decrease potency.
    • Iodination significantly reduces glucagon inactivation by plasma and liver membranes, increasing its plasma concentration and half-life.

    Conclusions:

    • Iodination enhances glucagon's intrinsic affinity for its receptors and adenylate cyclase.
    • Iodinated glucagon derivatives demonstrate improved metabolic stability and prolonged biological effects.
    • The degree of iodination critically influences glucagon's biological activity and stability.