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Related Experiment Videos

Evidence that three structural genes code for human alkaline phosphatases.

L E Seargeant, R A Stinson

    Nature
    |September 13, 1979
    PubMed
    Summary
    This summary is machine-generated.

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    Human alkaline phosphatases from liver, kidney, and bone share a common structural gene. This study distinguishes them from intestinal and placental forms, aiding tumor-associated enzyme classification.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • The genetic basis for human alkaline phosphatase (ALP) isoenzymes is not fully understood.
    • Previous studies suggest at least three genes for placental, intestinal, and liver/kidney/bone ALPs.
    • Distinguishing tumor-associated ALPs from normal tissue isoenzymes requires structural criteria.

    Purpose of the Study:

    • To investigate the structural basis of human alkaline phosphatase isoenzymes.
    • To determine if liver, kidney, and bone ALPs originate from the same structural gene.
    • To assess the utility of peptide mapping for classifying tumor-associated ALPs.

    Main Methods:

    • Employed a sensitive peptide-mapping technique.
    • Analyzed structural differences between human alkaline phosphatase isoenzymes.

    Related Experiment Videos

    Main Results:

    • Structural evidence indicates that alkaline phosphatases from liver, kidney, and serum (Paget's disease) are products of the same structural gene.
    • These isoenzymes are structurally distinct from intestinal and placental alkaline phosphatases.
    • Peptide mapping effectively differentiates these isoenzyme groups.

    Conclusions:

    • Human liver, kidney, and bone alkaline phosphatases likely arise from a single structural gene.
    • This finding helps clarify the genetic origins of ALP isoenzymes.
    • Peptide mapping is a valuable tool for the structural classification of tumor-associated alkaline phosphatases.