title: H-NMR characterization of the human myocardium myoglobin and erythrocyte hemoglobin signals.
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 degrees C and maintains a 3.9 ppm separation with the corresponding Hb A signal throughout the physiological temperature range. In the particular case of the human thenar muscle, the deoxy Mb signal is clearly detectable without any interference from Hb.
authors.affiliation: Biological Chemistry Department, University of California, Davis 95616-8635.
authors.forename: U
authors.initials: U
authors.lastname: Kreutzer
authors.forename: Y
authors.initials: Y
authors.lastname: Chung
authors.forename: D
authors.initials: D
authors.lastname: Butler
authors.forename: T
authors.initials: T
authors.lastname: Jue
mesh_terms: D000818:Animals; D001831:Body Temperature; D004912:Erythrocytes / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D006736:Horses; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D009206:Myocardium / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D010101:Oxygen Consumption
chemical_list: D006454:Hemoglobins; D009211:Myoglobin