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Spectroscopic studies on the interaction of riboflavin with bovine serum albumin

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Field Value
 
Title Spectroscopic studies on the interaction of riboflavin with bovine serum albumin
 
Creator Kamat, B P
Seetharamappa, J
Melwanki, M B
 
Subject Riboflavin
bovine serum albumin
fluorescent hydrophobic probe
fluorometric method
circular dichroism studies
 
Description 173-178
The mechanism of interaction of riboflavin (RF) with bovine serum albumin (BSA) using fluorometric and circular dichroism (CD) methods has been reported. The association constant (K) for RF-BSA binding shows that the interaction is non-covalent in nature. Stern-Volmer analysis of fluorescence quenching data shows that the fraction of fluorophore (BSA) accessible to the quencher (RF) is close to unity, indicating that both tryptophan residues of BSA are involved in the interaction. The high magnitude of rate constant for quenching kq (1013 M-1s-1) indicates that RF binding site is in close proximity to tryptophan residue of BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of RF to BSA predominantly involves the formation of hydrophobic bonds. Binding studies in the presence of a hydrophobic probe 8-anilino-1-naphthalene sulphonic acid, sodium salt (ANS) showed that RF and ANS do not share common sites in BSA. The small decrease in critical micellar concentration of anionic surfactant, sodium dodecyl sulphate in the presence of RF shows that ionic character of RF also contributes to binding and is not solubilized inside the micelle. Significant decrease in concentration of free RF has been observed in the presence of paracetamol. The CD spectrum shows the binding of RF leads to a change in the α helical structure of BSA.
 
Date 2009-04-02T06:16:23Z
2009-04-02T06:16:23Z
2004-08
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3702
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol.41(4) [August 2004]