Document Detail

Myoglobin oxygen dissociation by multiwavelength spectroscopy.
MedLine Citation:
PMID:  9029202     Owner:  NLM     Status:  MEDLINE    
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 degrees C, at pH 7.0. In addition, dissociation curves were determined at 37 degrees 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 degrees C. The myoglobin dissociation curve was well fit by the Hill equation [saturation = PO2/(PO2 + P50)].
K A Schenkman; D R Marble; D H Burns; E O Feigl
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of applied physiology (Bethesda, Md. : 1985)     Volume:  82     ISSN:  8750-7587     ISO Abbreviation:  J. Appl. Physiol.     Publication Date:  1997 Jan 
Date Detail:
Created Date:  1997-04-28     Completed Date:  1997-04-28     Revised Date:  2013-09-26    
Medline Journal Info:
Nlm Unique ID:  8502536     Medline TA:  J Appl Physiol (1985)     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  86-92     Citation Subset:  IM    
Department of Pediatrics, University of Wisconsin, Madison 53792, USA.
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MeSH Terms
Least-Squares Analysis
Myoglobin / metabolism*
Oxygen / metabolism*
Spectrum Analysis / methods*
Grant Support
Reg. No./Substance:
0/Myoglobin; 7782-44-7/Oxygen

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