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Related Experiment Videos

Diamine oxidase in the hen.

T Biegański, M A Ulatowska

    Agents and Actions
    |April 1, 1983
    PubMed
    Summary

    Hens possess diamine oxidase (histaminase) in their digestive tract, liver, and spleen. This enzyme

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Comparative Physiology

    Background:

    • Diamine oxidase (DAO) plays a crucial role in amine metabolism.
    • Understanding DAO distribution and properties is vital for metabolic research.

    Purpose of the Study:

    • To investigate the distribution and characteristics of diamine oxidase (histaminase) in adult hens.
    • To compare hen intestinal DAO with other species and identify its inhibitors.

    Main Methods:

    • Assaying diamine oxidase activity in various hen tissues (gastrointestinal tract, liver, spleen).
    • Characterizing the enzyme's localization (particle-bound) and reaction products in the intestine and liver.
    • Comparing inhibitor profiles of hen intestinal DAO with rat intestinal and pea seedling DAO.
    • Testing the inhibitory effects of natural dipeptides (carnosine, anserine) on hen intestinal DAO.

    Main Results:

    • Significant diamine oxidase activity was detected in the hen's gastrointestinal tract (ileum highest), liver, and spleen.
    • Intestinal DAO is primarily particle-bound, catalyzing putrescine oxidation to delta 1-pyrroline.
    • Liver DAO produces both delta 1-pyrroline and gamma-aminobutyric acid.
    • Hen intestinal DAO shares inhibitor properties with rat intestinal DAO but differs from pea seedling DAO.
    • Carnosine and anserine were identified as potent inhibitors of hen intestinal diamine oxidase.

    Conclusions:

    • Diamine oxidase is widely distributed in adult hen tissues, with a notable presence in the ileum.
    • Hen intestinal DAO exhibits distinct biochemical properties and inhibition patterns compared to plant-based enzymes.
    • Natural dipeptides carnosine and anserine effectively inhibit hen intestinal diamine oxidase, suggesting potential physiological roles.

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