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Methemoglobinemia

Mansouri, Ali, Lurie, Aubrey A.·1993·American Journal of Hematology
DOI 10.1002/ajh.2830420104
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Abstract

The ferrous iron of hemoglobin is exposed continuously to high concentrations of oxygen and, thereby, is oxidized slowly to methemoglobin, a protein unable to carry oxygen. To restore hemoglobin function, methemoglobin (ferrihemoglobin) must be reduced to hemoglobin (ferrohemoglobin). Under physiological conditions, methemoglobin reduction is accomplished mainly by red cell NADH‐cytochrome b 5 reductase (NADH‐methemoglobin reductase) so efficiently that there is insignificant amounts of methemoglobin in the circulating blood. However, should methemoglobin formation be increased—e.g., due to the presence of oxidant drugs, or an abnormal methemoglobin not amenable to reduction (hemoglobin M), or a deficiency in red cell cytochrome b 5 reductase—methemoglobinemia will result. Most methemoglobinemias have no adverse clinical consequences and need not be treated. Under certain conditions, such as exposure to large amounts of oxidant or in young infants, rapid treatment is necessary. In hereditary cytochrome b 5 deficiency, treatment is often directed at improving the poor cosmetic effect of persistent cyanosis with the minimum amount of drugs to give satisfactory clinical results. © 1993 Wiley‐Liss, Inc.

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Metadata

Authors
Mansouri, A., & Lurie, A. A.
Venue
American Journal of Hematology
Publisher
Wiley
Published
1993-01
Volume
42
Issue
1
Pages
7-12
ISSN
  • 0361-8609 (ISSN-L)
  • 1096-8652
DOI
10.1002/ajh.2830420104
OpenAlex
W96484744
Cited by
330
References
1
FWCI
5.00
Type
journal article
Language
en
Open access
closed
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4939 d)

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Mansouri, A., & Lurie, A. A. (1993). Methemoglobinemia. American Journal of Hematology. https://doi.org/10.1002/ajh.2830420104

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