Spectrophotometry of hydroxocobalamin and hemoglobin reveals production of an unanticipated methemoglobin variant

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Abstract

Introduction. Cyanide-poisoned patients often require pulse oximetry and co-oximetry to measure oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and methemoglobin. These and other critical laboratory measurements can be confounded by the cyanide antidote hydroxocobalamin. The postulated mechanism of this confounding is direct optical interference. Methods. The spectra of swine hemoglobin with and without hydroxocobalamin were measured from 450-800 nm. The resulting complex spectrum was divided into hemoglobin, hydroxocobalamin, and a remainder spectrum. Results. The remainder spectrum appears to be a methemoglobin variant quantitatively dependant on the amount of hydroxocobalamin added to the hemoglobin solution and the presence of oxygen. The Pearson's correlation coefficient comparing the known swine methemoglobin spectrum with the remainder spectrum reveals a very high degree of correlation (r2=0.986). Conclusion. This is the first study to document methemoglobin formation caused by hydroxocobalamin. Further studies are needed in vitro and in vivo to assess this previously unreported methemoglobin variant.

Original languageEnglish (US)
Pages (from-to)545-550
Number of pages6
JournalClinical Toxicology
Volume46
Issue number6
DOIs
StatePublished - Jul 2008

Fingerprint

Hydroxocobalamin
Methemoglobin
Spectrophotometry
Hemoglobins
Oximetry
Cyanides
Swine
Carboxyhemoglobin
Light interference
Antidotes
Oxyhemoglobins
Oxygen

Keywords

  • Cyanide
  • Hemoglobin
  • Hydroxocobalamin
  • Methemoglobin
  • Spectrophotometry

ASJC Scopus subject areas

  • Health, Toxicology and Mutagenesis
  • Toxicology

Cite this

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title = "Spectrophotometry of hydroxocobalamin and hemoglobin reveals production of an unanticipated methemoglobin variant",
abstract = "Introduction. Cyanide-poisoned patients often require pulse oximetry and co-oximetry to measure oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and methemoglobin. These and other critical laboratory measurements can be confounded by the cyanide antidote hydroxocobalamin. The postulated mechanism of this confounding is direct optical interference. Methods. The spectra of swine hemoglobin with and without hydroxocobalamin were measured from 450-800 nm. The resulting complex spectrum was divided into hemoglobin, hydroxocobalamin, and a remainder spectrum. Results. The remainder spectrum appears to be a methemoglobin variant quantitatively dependant on the amount of hydroxocobalamin added to the hemoglobin solution and the presence of oxygen. The Pearson's correlation coefficient comparing the known swine methemoglobin spectrum with the remainder spectrum reveals a very high degree of correlation (r2=0.986). Conclusion. This is the first study to document methemoglobin formation caused by hydroxocobalamin. Further studies are needed in vitro and in vivo to assess this previously unreported methemoglobin variant.",
keywords = "Cyanide, Hemoglobin, Hydroxocobalamin, Methemoglobin, Spectrophotometry",
author = "Denninghoff, {Kurt R} and Walter, {Frank G} and Langa, {A. J.} and Yao He and Chipman, {Russell A}",
year = "2008",
month = "7",
doi = "10.1080/15563650701846270",
language = "English (US)",
volume = "46",
pages = "545--550",
journal = "Clinical Toxicology",
issn = "1556-3650",
publisher = "Informa Healthcare",
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TY - JOUR

T1 - Spectrophotometry of hydroxocobalamin and hemoglobin reveals production of an unanticipated methemoglobin variant

AU - Denninghoff, Kurt R

AU - Walter, Frank G

AU - Langa, A. J.

AU - He, Yao

AU - Chipman, Russell A

PY - 2008/7

Y1 - 2008/7

N2 - Introduction. Cyanide-poisoned patients often require pulse oximetry and co-oximetry to measure oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and methemoglobin. These and other critical laboratory measurements can be confounded by the cyanide antidote hydroxocobalamin. The postulated mechanism of this confounding is direct optical interference. Methods. The spectra of swine hemoglobin with and without hydroxocobalamin were measured from 450-800 nm. The resulting complex spectrum was divided into hemoglobin, hydroxocobalamin, and a remainder spectrum. Results. The remainder spectrum appears to be a methemoglobin variant quantitatively dependant on the amount of hydroxocobalamin added to the hemoglobin solution and the presence of oxygen. The Pearson's correlation coefficient comparing the known swine methemoglobin spectrum with the remainder spectrum reveals a very high degree of correlation (r2=0.986). Conclusion. This is the first study to document methemoglobin formation caused by hydroxocobalamin. Further studies are needed in vitro and in vivo to assess this previously unreported methemoglobin variant.

AB - Introduction. Cyanide-poisoned patients often require pulse oximetry and co-oximetry to measure oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and methemoglobin. These and other critical laboratory measurements can be confounded by the cyanide antidote hydroxocobalamin. The postulated mechanism of this confounding is direct optical interference. Methods. The spectra of swine hemoglobin with and without hydroxocobalamin were measured from 450-800 nm. The resulting complex spectrum was divided into hemoglobin, hydroxocobalamin, and a remainder spectrum. Results. The remainder spectrum appears to be a methemoglobin variant quantitatively dependant on the amount of hydroxocobalamin added to the hemoglobin solution and the presence of oxygen. The Pearson's correlation coefficient comparing the known swine methemoglobin spectrum with the remainder spectrum reveals a very high degree of correlation (r2=0.986). Conclusion. This is the first study to document methemoglobin formation caused by hydroxocobalamin. Further studies are needed in vitro and in vivo to assess this previously unreported methemoglobin variant.

KW - Cyanide

KW - Hemoglobin

KW - Hydroxocobalamin

KW - Methemoglobin

KW - Spectrophotometry

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