Affiliation:
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
Abstract
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[Formula: see text] 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 =[Formula: see text]/([Formula: see text]+ P50)].
Publisher
American Physiological Society
Subject
Physiology (medical),Physiology
Cited by
135 articles.
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