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Heligmosomoides polygyrus: peroxidase activity.

C M Preston, J Barrett

    Experimental Parasitology
    |August 1, 1987
    PubMed
    Summary

    Mitochondrial peroxidase activity in Heligmosomoides polygyrus was highest with linoleic acid peroxide. This enzyme is functionally linked to cytochrome c within the electron transport chain.

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    Microbial ecology·2005

    Area of Science:

    • Biochemistry
    • Parasitology
    • Cellular Biology

    Background:

    • Heligmosomoides polygyrus is a nematode parasite.
    • Mitochondria are crucial organelles for cellular respiration.
    • Peroxidases play vital roles in cellular defense and metabolism.

    Purpose of the Study:

    • To investigate the localization and biochemical properties of peroxidase activity in Heligmosomoides polygyrus.
    • To determine the preferred electron donors for the mitochondrial peroxidase.
    • To elucidate the interaction of this peroxidase with the mitochondrial electron transport chain.

    Main Methods:

    • Subcellular fractionation to isolate mitochondria.
    • Enzyme assays using various electron donors (organic and inorganic peroxides).
    • Studies with electron transport chain substrates and inhibitors.

    Main Results:

    • Peroxidase activity was primarily localized to the mitochondrion.
    • The enzyme exhibited activity with hydrogen peroxide, cumene peroxide, and linoleic acid peroxide, with highest activity observed with linoleic acid peroxide.
    • Enzyme kinetics and inhibitor studies suggested a functional link to cytochrome c in the electron transport chain.

    Conclusions:

    • Heligmosomoides polygyrus possesses a mitochondrial peroxidase.
    • Linoleic acid peroxide is a preferred substrate.
    • The enzyme's interaction with the electron transport chain, potentially via cytochrome c, is significant for its function in vivo.

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