1H-NMR characterization of the human myocardium myoglobin and erythrocyte hemoglobin signais

Ulrike Kreutzer, Youngran Chung, Daniel Butler, Thomas Jue

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The 1H-NMR signal of deoxy Mb provides a unique opportunity to measure tissue oxygenation in vivo. To utilize the technique for human application, however, requires a specific spectral characterization of both human Mb and erythrocyte Hb. We report that the proximal histidyl-NH signal of human deoxy Mb resonates at 80.3 ppm at 25°C and maintains a 3.9 ppm separation with the corresponding Hb A signal throughout the physioiogical temperature range. In the particular case of the human thenar muscle, the deoxy Mb signal is clearly detectable without any interference from Hb.

Original languageEnglish (US)
Pages (from-to)33-37
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1161
Issue number1
DOIs
StatePublished - Jan 15 1993

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Oxygenation
Myoglobin
Muscle
Myocardium
Hemoglobins
Erythrocytes
Nuclear magnetic resonance
Tissue
Temperature
Muscles
Proton Magnetic Resonance Spectroscopy

Keywords

  • (Human heart)
  • Hemoglobin
  • Myoglobin
  • NMR, H-
  • Oxygen

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology
  • Medicine(all)

Cite this

1H-NMR characterization of the human myocardium myoglobin and erythrocyte hemoglobin signais. / Kreutzer, Ulrike; Chung, Youngran; Butler, Daniel; Jue, Thomas.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1161, No. 1, 15.01.1993, p. 33-37.

Research output: Contribution to journalArticle

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