Document Detail


The hemoglobin-oxygen equilibrium associated with subunit dissociation.
MedLine Citation:
PMID:  836868     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The effect of oxygen-linked tetramer-dimer dissociation on oxygen equilibrium of hemoglobin was investigated by measuring the equilibrium curves over a wide range of protein concentration. A Hill scheme which takes the subunit dissociation into account describes well the overall concentration dependences of the oxygen pressure and slope of the Hill plot at half saturation. Values of dissociation constant for oxyhemoglobin estimated from the equilibrium data agree with the vaues measured by other methods for phosphate-free and diphosphoglycerate-added hemoglobin. The present results indicate that oxygen equilibrium properties are only slightly influenced bysubunit dissociation in the concentration range above 60 muM (as heme) at which most equilibrium experiments have been carried out.
Authors:
K Imai; H Yonetani
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  490     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1977 Jan 
Date Detail:
Created Date:  1977-04-15     Completed Date:  1977-04-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  164-70     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Diphosphoglyceric Acids / blood
Humans
Kinetics
Oxygen / blood*
Oxyhemoglobins / metabolism*
Phytic Acid / blood
Protein Conformation
Structure-Activity Relationship
Chemical
Reg. No./Substance:
0/Diphosphoglyceric Acids; 0/Oxyhemoglobins; 7782-44-7/Oxygen; 83-86-3/Phytic Acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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