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Dissection of the radical reactions linked to fetal hemoglobin reveals enhanced pseudoperoxidase activity
In the presence of excess hydrogen peroxide (H(2)O(2)), ferrous (Fe(+2)) human hemoglobin (Hb) (α2β2) undergoes a rapid conversion to a higher oxidation ferryl state (Fe(+4)) which rapidly autoreduces back to the ferric form (Fe(+3)) as H(2)O(2) is consumed in the reaction. In the presence of additi...
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| Gepubliceerd in: | Front Physiol |
|---|---|
| Hoofdauteurs: | , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Frontiers Media S.A.
2015
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4335259/ https://ncbi.nlm.nih.gov/pubmed/25750627 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3389/fphys.2015.00039 |
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