| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1988440 | Journal of Biochemical and Biophysical Methods | 2007 | 5 Pages |
Abstract
The interactions between loratadine and bovine serum albumin (BSA) and human serum albumin (HSA) were studied using tryptophan fluorescence quenching method. The fluorescence intensity of the two serum albumins could be quenched 70% at the molar ratio [loratadine]:[BSA (or HSA)] = 10:1. In the linear range (0–50 μmol L− 1) quenching constants were calculated using Stern–Volmer equation. Temperature in the range 298 K–310 K had a significant effect (p < 0.05) on the two serum albumins through ANOVA analysis and t-test. Furthermore the conformation changes in the interactions were studied using FTIR spectroscopy.
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Authors
Bo Zhou, Zu-De Qi, Qi Xiao, Jia-Xin Dong, Ye-Zhong Zhang, Yi Liu,