Document Detail


Kinetics of the conformational changes of hemopexin in acid media.
MedLine Citation:
PMID:  12715     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Under the action of acid media the hemopexin molecule unfolds with resulting heme expulsion from the binding site, followed by heme dimerization and reassociation of dimeric heme with the unfolded protein molecule. The rate of the reaction is pH dependent and the whole process is fully reversible for a certain time interval. Prolonged treatment of hemopexin at acidic conditions, however, leads to the irreversible denaturation of this protein.
Authors:
Z Hrkal; M B Kodícek; Z Vodrázka
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Annals of clinical research     Volume:  8 Suppl 17     ISSN:  0003-4762     ISO Abbreviation:  Ann. Clin. Res.     Publication Date:  1976  
Date Detail:
Created Date:  1977-02-16     Completed Date:  1977-02-16     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  0220042     Medline TA:  Ann Clin Res     Country:  FINLAND    
Other Details:
Languages:  eng     Pagination:  239-43     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Heme / metabolism
Hemopexin* / isolation & purification
Humans
Hydrogen-Ion Concentration
Protein Binding
Protein Conformation
Spectrophotometry, Atomic
Chemical
Reg. No./Substance:
14875-96-8/Heme; 9013-71-2/Hemopexin

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


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