Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10561397 | Talanta | 2005 | 6 Pages |
Abstract
The interactions between proteins and Ponceau 4R (PR) in aqueous solution have been studied by the techniques of resonance light scattering (RLS) spectroscopy, the absorption spectroscopy, zeta potential assay and circular dichroism (CD) spectrum. The dry PR can assemble on the surface of protein via electrostatic and hydrophobic forces to produce an associated compound of protein-PR, this compound can enhance the RLS of protein. Based on this fact, a simple, rapid, and sensitive method has been developed for the determination of proteins at nanogram level by RLS technique with a common spectrofluorimeter. Under optimum conditions, the linear range is 0.10-39.2 μg mLâ1 for the determination of both bovine serum albumin (BSA) and human serum albumin (HSA). The detection limits (S/N = 3) are 6.96 ng mLâ1 for BSA and 5.71 ng mLâ1 for HSA, respectively. There is almost no interference from amino acids, most of the metal ions, and other coexistent substances. The method has been satisfactorily applied to the direct determination of the total protein in human serum.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Hui Zhong, Jing-Juan Xu, Hong-Yuan Chen,