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Lysoplasmalogenase--a microsomal enzyme from rat brain

J Gunawan, H Debuch

    Journal of Neurochemistry
    |September 1, 1982
    PubMed
    Summary

    Researchers identified a novel rat brain enzyme activity that releases free aldehydes from lyso-plasmalogen. This enzyme shows peak activity in young rats and is sensitive to pH and inhibitors.

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    Biochemical Society transactions·1992

    Area of Science:

    • Biochemistry
    • Neuroscience
    • Enzymology

    Background:

    • Plasmalogens are a unique class of phospholipids with a vinyl ether linkage.
    • Lysoplasmalogens are intermediates in plasmalogen metabolism.
    • The enzymatic pathways for plasmalogen degradation are not fully elucidated.

    Purpose of the Study:

    • To characterize a novel enzymic activity in rat brain.
    • To investigate the substrate specificity of this enzyme.
    • To determine the optimal conditions and inhibitors for this enzymatic activity.

    Main Methods:

    • Preparation of microsomal fractions from rat brains of various ages.
    • Incubation of [1-14C]alk-1'-enyl-sn-glycero-3-phosphoethanolamine (lyso-plasmalogen) with enzyme fractions.
    • Measurement of radioactive free aldehyde release.
    • Testing the effect of enzyme concentration, substrate concentration, incubation time, pH, bivalent cations, and detergents.

    Main Results:

    • A specific enzymic activity was found in rat brain microsomal fractions that liberates free aldehydes from lyso-plasmalogen.
    • The highest specific enzyme activity was observed in 21-day-old rats.
    • Enzyme activity was dependent on enzyme and substrate concentrations and linear up to 60 min.
    • The pH optimum was between 7.1 and 7.3.
    • Bivalent cations (Mg2+, Ca2+) and detergents inhibited the reaction.
    • No activity was detected with acylated plasmalogens or ox corpus callosum plasmalogen.

    Conclusions:

    • Rat brain possesses a distinct enzymatic activity capable of cleaving the vinyl ether bond in lyso-plasmalogen.
    • This enzyme activity is developmentally regulated, with peak activity in young animals.
    • The enzyme's properties suggest a specific role in the metabolism of alkenyl phospholipids.

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