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1 Department of Pediatrics, University of Wisconsin, Madison, Wisconsin 53792; 2 Departments of Bioengineering and Physiology, University of Washington, Seattle, Washington 98195; and 3 Department of Chemistry, McGill University, Montreal, Quebec, Canada H3A 2K6
Received 13 March 1996; accepted in final form 21 August 1996.
Schenkman, Kenneth A., David R. Marble, David H. Burns, and
Eric O. Feigl. Myoglobin oxygen dissociation by multiwavelength spectroscopy. J. Appl. Physiol. 82(1):
86-92, 1997.
Multiwavelength optical spectroscopy was used to
determine the oxygen-binding characteristics for equine myoglobin.
Oxygen-binding relationships as a function of oxygen tension were
determined for temperatures of 10, 25, 35, 37, and 40°C, at pH 7.0. In addition, dissociation curves were determined at 37°C for pH
6.5, 7.0, and 7.5. Equilibration was achieved with a myoglobin
solution, at the desired temperature and pH, and 16 oxygen-nitrogen gas
mixtures of known oxygen fraction. Correction for the inevitable
presence of metmyoglobin was made by using a three-component least
squares analysis and by correcting the end point oxymyoglobin spectra
for the presence of metmyoglobin. The
PO2 at which myoglobin is
half-saturated with O2 (P50) was determined to be 2.39 Torr at pH 7.0 and 37°C. The myoglobin dissociation
curve was well fit by the Hill equation [saturation = PO2/(PO2 + P50)].
equilibration; metmyoglobin; least squares analysis; second derivative
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