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Related Experiment Videos

Dipeptide absorption in man.

M D Hellier, C D Holdsworth, I McColl

    Gut
    |December 1, 1972
    PubMed
    Summary
    This summary is machine-generated.

    Intact dipeptide transport in the human intestine was studied. Dipeptides like glycyl-glycine were absorbed faster than free amino acids, indicating intact peptide absorption and subsequent hydrolysis.

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    Area of Science:

    • Gastroenterology
    • Human Physiology
    • Nutritional Science

    Background:

    • The intestinal absorption of peptides is crucial for protein digestion and amino acid uptake.
    • Understanding the transport mechanisms of dipeptides is essential for nutritional science and clinical applications.

    Purpose of the Study:

    • To investigate the intestinal absorption of dipeptides (glycyl-glycine, glycyl-l-alanine, glycyl-l-lysine) in humans.
    • To determine whether dipeptides are absorbed intact or hydrolyzed prior to absorption.

    Main Methods:

    • Quantitative perfusion method used in normal subjects.
    • Measurement of constituent amino acids in the intestinal lumen during dipeptide absorption.
    • Analysis of portal blood for dipeptides and constituent amino acids.

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    Main Results:

    • Glycyl-glycine and glycyl-l-alanine were absorbed faster as dipeptides than as free amino acids, suggesting intact transport.
    • Lumenal amino acids detected during absorption may represent back-diffusion after intact dipeptide uptake.
    • Glycyl-l-lysine, known for intact transport, was hydrolyzed to constituent amino acids before reaching portal venous blood.

    Conclusions:

    • The human intestine can transport dipeptides intact, leading to faster amino acid absorption compared to free amino acids.
    • Hydrolysis of some dipeptides occurs either within the intestinal cells or during their passage into the portal circulation.
    • These findings highlight the complex mechanisms of dipeptide absorption and metabolism in the human gut.