| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 596600 | Colloids and Surfaces A: Physicochemical and Engineering Aspects | 2008 | 5 Pages |
Abstract
The interaction between colloidal TiO2 and bovine serum albumin (BSA) was studied by using absorption and fluorescence spectroscopic methods. The quenching of the intrinsic protein fluorescence in the presence of different concentrations of colloidal TiO2 was analyzed and number of binding sites (n) and apparent binding constant (K) were measured. The quenching mechanism of albumin by colloidal TiO2 is discussed. The energy transfer efficiency (E) and critical transfer distance (R0) were determined.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
A. Kathiravan, R. Renganathan,