a(CHEBI:Peroxidase)
It is well known that in the presence of H2O2 hemoglobin exhibits a peroxidase-like activity, catalyzed by the heme moiety. PubMed:28088643
However, no changes in peroxidase activity were observed after incubation with haptoglobin or hemopexin (Fig. 2). PubMed:28088643
At the same time, heme bound to NEAT does not catalyze the peroxidase reaction due to inability to interact with H2O2. PubMed:28088643
Our data demonstrate a significant decrease in peroxidase activity of hemoglobin incubated with NEATHP, indicating heme transfer. PubMed:28088643
Therefore, we demonstrated that an active scavenging of heme by NEAT can reduce peroxidase activity of hemoglobin, whereas passive scavengers cannot. PubMed:28088643
Moreover, heme scavenging by NEAT-HP markedly decreased hemoglobin-mediated peroxidase activity (Fig. 2), whereas haptoglobin was capable of only a small attenuation of peroxidase activity and hemopexin did not affect it at all. PubMed:28088643
However, no changes in peroxidase activity were observed after incubation with haptoglobin or hemopexin (Fig. 2). PubMed:28088643
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.