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Alkaline phosphatase in mitochondria.

P D Wilson, L M Franks, D C Cottell

    Cell Biology International Reports
    |January 1, 1977
    PubMed
    Summary
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    Mitochondria in mouse liver cells contain alkaline phosphatase, an enzyme also found on bile canaliculi membranes. This mitochondrial enzyme exhibits a unique isoenzyme pattern, distinct from the membrane-associated form.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Enzymology

    Background:

    • Alkaline phosphatase (AP) is a hydrolase enzyme crucial in various cellular processes.
    • Its localization and specific forms within liver cells are not fully elucidated.

    Purpose of the Study:

    • To investigate the presence and characteristics of alkaline phosphatase within mouse liver mitochondria.
    • To differentiate mitochondrial AP from plasma membrane-associated AP.

    Main Methods:

    • Electron microscopy with cytochemical staining for AP activity.
    • Biochemical assays to quantify AP activity in subcellular fractions.
    • Starch gel electrophoresis and neuraminidase treatment to analyze isoenzyme patterns.

    Main Results:

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    • AP activity was detected in liver cell mitochondria and on bile canaliculi plasma membranes.
    • Mitochondrial AP was partially inhibited by L-phenylalanine and Levamisole.
    • Plasma membrane AP was completely inhibited by Levamisole.
    • Mitochondrial AP displayed a distinct isoenzyme pattern (3 bands) resistant to neuraminidase.
    • Supernatant AP showed a single band sensitive to neuraminidase.

    Conclusions:

    • Mouse liver mitochondria harbor a distinct form of alkaline phosphatase.
    • This mitochondrial AP differs biochemically and electrophoretically from the plasma membrane-associated enzyme.
    • The findings contribute to understanding the tissue-specific localization and heterogeneity of alkaline phosphatase.