Document Detail


Heat denaturation of serum albumin monitored by 1-anilino-naphthalene-8-sulfonate.
MedLine Citation:
PMID:  7378445     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The process of heat denaturation of serum albumin, and the properties of several denatured components of albumin were studied using 1-anilino-naphthalene-8-sulfonate as a probe dye. Like native albumin, these protein species all induce fluorescence of the dye with maximum emission at 470 nm when excited at 380 nm. However, the affinity of albumin for the dye decreased on denaturation. This fluorescent dye bound competitively to both native and denatured albumin with another probe dye, 2-(4'-hydroxyphenylazo)benzoic acid, has a specific absorption band at about 480 nm on binding with native albumin. Fatty acids, such as lauric acid, inhibited the interaction of 1-anilinonaphthalene-8-sulfonate with native albumin, but had little effect on its binding with denatured albumin.
Authors:
H Terada; K Hiramatsu; K Aoki
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  622     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1980 Apr 
Date Detail:
Created Date:  1980-08-28     Completed Date:  1980-08-28     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  161-70     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Anilino Naphthalenesulfonates*
Animals
Cattle
Hot Temperature
Protein Binding
Protein Conformation
Protein Denaturation
Serum Albumin, Bovine*
Spectrometry, Fluorescence
Thermodynamics
Chemical
Reg. No./Substance:
0/Anilino Naphthalenesulfonates; 0/Serum Albumin, Bovine

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


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