| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 613528 | Journal of Colloid and Interface Science | 2006 | 8 Pages |
Abstract
In this work, bovine hemoglobin (Hb) has been studied mainly by the fluorescence method. pH has been found to exert a profound effect on Hb structure. This has been confirmed by fluorescence and circular dichroism (CD) studies. The pH-induced change in quaternary structure of Hb indirectly affects its secondary structure. This in turn affects ligand binding to Hb at various pH. The binding of two amphiphiles, a bile salt and a surfactant, have been investigated. The pH-induced structural modification of Hb has been confirmed by studies with the well-known denaturant urea and the polarity probe ANS, which has been used as an extrinsic fluorophore.
Related Topics
Physical Sciences and Engineering
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Authors
Swati De, Agnishwar Girigoswami,