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Related Experiment Videos

Developmental change in human intestinal alkaline phosphatase.

R A Mulivor, V L Hannig, H Harris

    Proceedings of the National Academy of Sciences of the United States of America
    |August 1, 1978
    PubMed
    Summary

    Human alkaline phosphatases from fetal and adult tissues were analyzed. The fetal intestinal enzyme differs from the adult form, suggesting developmental changes in enzyme synthesis or modification.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Developmental Biology

    Background:

    • Alkaline phosphatases (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.1) are crucial enzymes with diverse tissue-specific expression.
    • Differences in alkaline phosphatase isoforms have been observed between fetal and adult tissues, particularly in the intestine.

    Purpose of the Study:

    • To investigate biochemical differences between fetal and adult human alkaline phosphatases from various tissues.
    • To characterize the fetal intestinal alkaline phosphatase and compare it to the adult form.

    Main Methods:

    • Starch gel electrophoresis was employed to analyze enzyme mobility.
    • Enzyme inhibition studies were conducted using various amino acids and dipeptides.
    • Treatment with neuraminidase was used to assess glycosylation differences.

    Main Results:

    • No electrophoretic or inhibition differences were found between fetal and adult alkaline phosphatases from liver, kidney, or bone.
    • Fetal intestinal alkaline phosphatase exhibited greater anodal mobility and neuraminidase sensitivity compared to the adult form.
    • The transition from fetal to adult intestinal alkaline phosphatase synthesis occurs around 28-32 weeks of gestation.

    Conclusions:

    • Fetal and adult intestinal alkaline phosphatases are distinct molecular entities.
    • These differences may arise from the expression of different gene loci or post-translational modifications, such as glycosylation.

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