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Interaction of bromocresol green with different serum albumins studied by fluorescence quenching
Author(s) -
Trivedu V. D.,
Saxena I.,
Siddiqui M. U.,
Qasim M. A.
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203751
Subject(s) - bromocresol green , bromocresol purple , chemistry , bovine serum albumin , ionic strength , quenching (fluorescence) , serum albumin , scatchard plot , fluorescence , binding constant , chromatography , binding site , biochemistry , organic chemistry , physics , quantum mechanics , aqueous solution
The binding of bromocresol green to bovine serum albumin at micromolar concentrations leads to quenching of protein fluorescence. This property has been used here to study interaction of bromocresol green with bovine serum albumin as a function of pH and ionic strength. The transformation of fluorescence quench data obtained with bromocresol green into Scatchard plots yielded an association constant of 3.06×107 1M‐1 and a binding capacity of about 1.0. The affinity of bromocresol green for bovine serum albumin remains virtually unchanged between pH 4.0 and 8.0 but decreases by about 7 fold with increase in ionic strength from 0.01 to 1.0. Six other serum albumins obtained from cat, dog, human, pig and sheep have also been studied for bromocresol green binding. Although all the albumins studied bind bromocresol green, they show considerable differences in their affinities towards the dye. It appears that despite a great degree of overall similarity in their structure and conformation, serum albumins from different species differ in their ligand binding properties.