Articles written in Journal of Chemical Sciences
Volume 99 Issue 4 October 1987 pp 273-279 Physical and Theoretical
Two classes of binding sites, a single high-affinity site with an association constant of 4·8×106 M−1 and two low-affinity sites with association constant of about 0·05×106 M−1 have been observed in the interaction of Naproxen with bovine serum albumin (BSA). Chemical modification of two tryptophan residues in BSA with 2-hydroxy-5-nitrobenzyl bromide has led to a reduction in the association constant of the high-affinity site by 89% and its number of binding sites by 66% suggesting the involvement of tryptophan residues in the high-affinity site. In contrast, the two low-affinity sites were not affected by the modification. Binding of Naproxen to the low-affinity sites of BSA induces microdisorganisation of the albumin structure leading to conformational changes as evident from fluorescence measurements with 1-anilino-8-naphthalenesulphonic acid as the probe.
Volume 105 Issue 4-5 August 1993 pp 279-285 Physical and Theoretical
The binding of rose bengal (RB) to bovine serum albumin (BSA) occurs with both the folded (at
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