Heligmosomoides polygyrus: peroxidase activity
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Updated: Sep 21, 2026

Detecting, Visualizing and Quantitating the Generation of Reactive Oxygen Species in an Amoeba Model System
Published on: November 5, 2013
Abstract:
Peroxidase activity in Heligmosomoides polygyrus was located primarily in the mitochondrion. The enzyme was active with a range of organic and inorganic electron donors and, in addition to hydrogen peroxide, it could utilize cumene peroxide, but the highest activity was obtained with linoleic acid peroxide. The effects of electron chain substrates and inhibitors on H. polygyrus mitochondrial peroxidase activity was consistent with the enzyme being linked functionally to cytochrome c, although in vivo, this may not be the only electron donor. The interaction of the peroxidase with electron transport is discussed.

