Proteins Fluorescence Quenching by [Hg(SCN)4]2- and Its Analytical Application

doi:10.3969/j.issn.0251-0790.2012.01.010

Abstract

Abstract: [Hg(SCN)₄]^2- in acidic medium of pH=1.4-3.4 could react with proteins, including bovine serum albumin(BSA), γ-globin(γ-G) and hemoglobin(Hb), to form complexes. As a result, the fluorescence intensities of the proteins were significantly quenched. The quenched fluorescence intensities(ΔF) in a certain range were linearly related to the concentration of Hg(Ⅱ), and the detection limit(3σ) were 4.4 ng/mL(BSA), 6.5 ng/mL(γ-G) and 12.9 ng/mL(Hb), respectively. The effects of the interaction on the fluorescence spectral characteristics of these complexes, suitable reaction conditions and influencing factors were investigated. The quenching mechanism was studied by absorption spectroscopy, binding constant and corresponding thermodynamic parameters at different temperatures. Some potential interferents on the assay by BSA were investigated. The method displayed good selectivity and was satisfactorily applied to the determination of asceptichrome in mercurochrome solution and thiomersalatum in HB-vaccine.

Key words: [Hg(SCN)₄]^2-, Bovine serum albumin(BSA), γ-Globin(γ-G), Hemoglobin(Hb), Fluorescence quenching

CLC Number:

O657

TrendMD:

TIAN Lun-Fu, LIU Zhong-Fang, HU Xiao-Li, KONG Ling, LIU Shao-Pu. Proteins Fluorescence Quenching by [Hg(SCN)₄]^2- and Its Analytical Application[J]. Chem. J. Chinese Universities, 2012, 33(01): 59.

References

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Proteins Fluorescence Quenching by [Hg(SCN)₄]^2- and Its Analytical Application

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