Document Detail


Oxygen equilibrium of hemoglobin J Cape Town.
MedLine Citation:
PMID:  5090068     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Polycythemia in carriers of hemoglobin J Cape Town or hemoglobin Chesapeake is thought to be produced by increased oxygen affinity of their blood. Both hemoglobins involve substitution of amino acid residue alpha FG-4. Measurements reported here, of the oxygen equilibrium of purified hemoglobin J Cape Town, permit direct comparison of the two hemoglobins. J Cape Town exhibits lower oxygen affinity, and greater heme-heme interaction, than Chesapeake; both exhibit normal Bohr effects. Substitution of one polar amino acid residue for another of opposite charge (arginine --> glutamic acid) thus appears to create less disruption of the interface between alpha- and beta-chains than substitution of a nonpolar residue (arginine --> leucine).
Authors:
S Charache; T Jenkins
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of clinical investigation     Volume:  50     ISSN:  0021-9738     ISO Abbreviation:  J. Clin. Invest.     Publication Date:  1971 Jul 
Date Detail:
Created Date:  1971-08-13     Completed Date:  1971-08-13     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7802877     Medline TA:  J Clin Invest     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1554-5     Citation Subset:  AIM; IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Blood Protein Electrophoresis
Heme / metabolism
Hemoglobins, Abnormal / metabolism*
Humans
Hydrogen-Ion Concentration
Oxygen / blood*
Polycythemia / blood*
Chemical
Reg. No./Substance:
0/Hemoglobins, Abnormal; 14875-96-8/Heme; 7782-44-7/Oxygen
Comments/Corrections

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


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