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Development of a reference material for alkaline phosphatase.

P H Duncan, S S McKneally, M L MacNeil

    Clinical Chemistry
    |January 1, 1984
    PubMed
    Summary
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    Developing a reference material for alkaline phosphatase (ALP) is feasible using liver, bone, or intestinal isoenzymes. The liver isoenzyme was selected for its availability and commutability with human serum ALP.

    Area of Science:

    • Biochemistry
    • Clinical Chemistry
    • Enzymology

    Background:

    • Alkaline phosphatase (ALP) is a crucial enzyme in human physiology.
    • Accurate measurement of ALP requires reliable reference materials.
    • Different human tissues express distinct ALP isoenzymes with varying properties.

    Purpose of the Study:

    • To evaluate the suitability of different human alkaline phosphatase (ALP) isoenzymes for use in a reference material.
    • To assess the stability, kinetic properties, and commutability of purified ALP isoenzymes from various human tissues.
    • To identify the optimal isoenzyme source for developing a stable and commutable ALP reference material.

    Main Methods:

    • Purification of alkaline phosphatase (ALP) isoenzymes from human liver, intestine, bone, and placenta.

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  • Determination of Michaelis constants (Km) for each isoenzyme preparation.
  • Assessment of response-surface patterns to evaluate commutability with human serum specimens.
  • Temperature-accelerated degradation studies to assess enzyme stability.

    • Main Results:

    • Kinetic properties (Km) of liver, bone, and intestinal ALP isoenzymes closely matched those in human serum.
    • Placental ALP isoenzyme exhibited significantly different kinetic properties and poor commutability.
    • All four isoenzymes demonstrated satisfactory stability under accelerated degradation conditions.
    • Liver, bone, and intestinal isoenzymes showed similar response-surface patterns, indicating good commutability.

    Conclusions:

    • Reference materials for alkaline phosphatase (ALP) can be effectively developed using liver, bone, or intestinal isoenzymes.
    • The liver isoenzyme is a suitable choice due to ease of acquisition, abundance, and excellent commutability with serum ALP.
    • The selected liver-derived reference material is stable, free from interfering enzymes, and commutable with human serum ALP.