Document Detail

Effects of oxidation on changes of compressibility of bovine serum albumin.
MedLine Citation:
PMID:  15113119     Owner:  NLM     Status:  MEDLINE    
The methods of ultrasound velocity and density measurements were used to study the adiabatic compressibility of bovine serum albumin (BSA) during its oxidation by the prooxidants Cu2+ and 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH). We did not find changes of compressibility of BSA in the presence of copper ions at rather high molar ratio Cu2+/BSA = 0.66 mol/mol. This can be explained by binding of the Cu2+ to the binding site of BSA and thus protecting the prooxidant action of the copper. However, AAPH-mediated oxidation of BSA resulted in an increase of its apparent specific compressibility (psik/beta0). These changes could be caused by the fragmentation of the protein.
T Hianik; P Rybár; Z Benediktyová; L Svobodová; A Hermetter
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  General physiology and biophysics     Volume:  22     ISSN:  0231-5882     ISO Abbreviation:  Gen. Physiol. Biophys.     Publication Date:  2003 Dec 
Date Detail:
Created Date:  2004-04-28     Completed Date:  2004-08-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8400604     Medline TA:  Gen Physiol Biophys     Country:  Slovakia    
Other Details:
Languages:  eng     Pagination:  467-76     Citation Subset:  IM    
Department of Biophysics and Chemical Physics, Faculty of Mathematics, Physics and Computer Science, Comenius University, Bratislava, Slovakia.
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MeSH Terms
Amidines / chemistry*
Copper / chemistry*
Densitometry / methods
Serum Albumin, Bovine / analysis,  chemistry*
Suspensions / chemistry
Ultrasonography / methods
Reg. No./Substance:
0/Amidines; 0/Serum Albumin, Bovine; 0/Suspensions; 13217-66-8/2,2'-azobis(2-amidinopropane); 7440-50-8/Copper

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

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