Journal
DYES AND PIGMENTS
Volume 73, Issue 2, Pages 211-216Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.dyepig.2005.11.008
Keywords
bovine serum albumin; bromopyrogallol red; spectroscopic studies
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The mechanism of binding of bromopyrogallol red (BPR) with bovine serum albumin (BSA) was investigated by fluorescence, absorption, circular dichroisna (CD) and lifetime measurements. The analysis of fluorescence data indicated the presence of both dynamic and static quenching mechanism in the binding. Various binding parameters have been evaluated. The CD spectral data revealed the decrease in a-helical content of BSA from 70.7% (in free BSA) to 53.89% (in bound form) thereby indicating the conformational change in BSA upon binding. The thermodynamic parameters have also been evaluated. The binding average distance, r between the donor (BSA) and acceptor (BPR) was determined based on the Forster's theory and it was found to be 3.84 nm. The association constant of BPR-BSA decreased in the presence of common ions. (c) 2005 Published by Elsevier Ltd.
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