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Am J Physiol Regul Integr Comp Physiol 282: R267-R272, 2002; doi:10.1152/ajpregu.00240.2001
0363-6119/02 $5.00
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Vol. 282, Issue 1, R267-R272, January 2002

Detection of myoglobin desaturation in Mirounga angustirostris during apnea

Paul J. Ponganis1, Ulrike Kreutzer2, Napapon Sailasuta3, Torre Knower1, Ralph Hurd3, and Thomas Jue2

1 Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla 92093-0204; 2 Department of Biological Chemistry, University of California, Davis 95616-8635; and 3 GE Medical Systems, Fremont, California 94539

1H NMR solution-state study of elephant seal (Mirounga angustirostris) myoglobin (Mb) and hemoglobin (Hb) establishes the temperature-dependent chemical shifts of the proximal histidyl Ndelta H signal, which reflects the respective intracellular and vascular PO2 in vivo. Both proteins exist predominantly in one major isoform and do not exhibit any conformational heterogeneity. The Mb and Hb signals are detectable in M. angustirostris tissue in vivo. During eupnea M. angustirostris muscle maintains a well-saturated MbO2. However, during apnea, the deoxymyoglobin proximal histidyl Ndelta H signal becomes visible, reflecting a declining tissue PO2. The study establishes a firm methodological basis for using NMR to investigate the metabolic responses during sleep apnea of the elephant seal and to secure insights into oxygen regulation in diving mammals.

nuclear magnetic resonance; oxygen; hypoxia; seal; apnea; eupnea


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