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Related Experiment Videos

On the difference between colonic and small intestinal alkaline phosphatase.

W C Griffiths, R Lev, J Gentile

    Clinical Biochemistry
    |August 1, 1985
    PubMed
    Summary

    Colonic and small intestinal alkaline phosphatase (ALP) share similar properties but differ in their molecular forms. Differences in electrophoretic mobility are likely due to varying proportions of these shared ALP forms.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Gastrointestinal Physiology

    Background:

    • Alkaline phosphatase (ALP) is a crucial enzyme found in various tissues, including the colon and small intestine.
    • Previous studies reported differences in the electrophoretic mobility of ALP from these two sources.

    Purpose of the Study:

    • To investigate the biochemical and electrophoretic properties of colonic and small intestinal alkaline phosphatase.
    • To elucidate the source of observed differences in cellulose acetate electrophoretic mobility.

    Main Methods:

    • Biochemical analysis of alkaline phosphatase extracts.
    • Electrophoretic separation on cellulose acetate.
    • Enzyme activity assays with L-phenylalanine and tetramisole.
    • Treatment with neuraminidase.

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    Main Results:

    • Both colonic and small intestinal alkaline phosphatase (ALP) were inhibited by L-phenylalanine and resistant to tetramisole.
    • Neuraminidase treatment altered a minor fraction of small intestinal ALP and the major portion of colonic ALP to a cathodically migrating form.
    • These findings suggest that both enzymes are composed of similar multiple forms.

    Conclusions:

    • Colonic and small intestinal alkaline phosphatase are likely mixtures of the same multiple enzyme forms.
    • The observed differences in electrophoretic mobility are attributed to variations in the proportions of these shared forms between the colon and small intestine.