Document Detail


Optical Spectroscopic Exploration of Binding of Cochineal Red-A with Two Homologous Serum Albumins.
MedLine Citation:
PMID:  22397587     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Cochineal Red-A is a, negatively charged, synthetic azo food colorant and a potential carcinogen. We present here the study of binding of Cochineal Red-A with two homologous serum albumins (SA), HSA and BSA, in aqueous pH 7.4 buffer using optical spectroscopic techniques. Protein intrinsic fluorescence quenching by Cochineal Red-A occurs through ground-state static interaction and its binding with BSA is stronger than with HSA. The magnitudes of thermodynamic parameters suggest that dye binding occurs principally via electrostatic complexation. Site-marker competitive binding shows that Cochineal Red-A binds primarily to site-I of SAs. CD spectra indicate that dye binding results in some conformational modification of SAs. Increase of ionic strength of medium results in lowering of binding. This study provides an important insight into possible means of removal of dye toxicity.
Authors:
Priyanka Bolel; Niharendu Mahapatra; Mintu Halder
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-3-7
Journal Detail:
Title:  Journal of agricultural and food chemistry     Volume:  -     ISSN:  1520-5118     ISO Abbreviation:  -     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-3-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0374755     Medline TA:  J Agric Food Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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