2009Wuji huaxue xuebaoRequires access

Interaction of Pb(II) with Bovine Serum Albumin under UV Irradiation

Hai Zhang

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Abstract

The interaction between Pb(Ⅱ)and bovine serum albumin(BSA)under the effect of UV C(253.7nm)irradiation at physiological condition have been investigated by UV spectrum,ultraviolet second-derivative spectroscopy and fluorescence spectrum.The research results indicated that UV C irradiation make the environments of aromatic residues change according to UV spectrum and ultraviolet second-derivative spectroscopy.Stern-Volmer equation and Lineweaver-Burk equation showed that the fluorescence quenching of BSA by Pb(Ⅱ)is also a static quenching procedure and strong binding site is not change after UV C irradiation.When adding Pb(Ⅱ)to irradiated BSA,the binding constant(KS)decreased gradually;while irradiating the mixture of Pb(Ⅱ)-BSA,the binding constant(KS)increased.

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What this paper is about

The interaction between Pb(Ⅱ)and bovine serum albumin(BSA)under the effect of UV C(253.7nm)irradiation at physiological condition have been investigated by UV spectrum,ultraviolet second-derivative spectroscopy and fluorescence spectrum.The research results indicated that UV C irradiation make the environments of aromatic residues change according to UV spectrum and ultraviolet second-derivative spectroscopy.Stern-Volmer equation and Lineweaver-Burk equation showed that the fluorescence quenching of BSA by Pb(Ⅱ)is also a static quenching procedure and strong binding site is not change after UV C irradiation.When adding Pb(Ⅱ)to irradiated BSA,the binding constant(KS)decreased gradually;while irradiating the mixture of Pb(Ⅱ)-BSA,the binding constant(KS)increased.

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Available abstract

The interaction between Pb(Ⅱ)and bovine serum albumin(BSA)under the effect of UV C(253.7nm)irradiation at physiological condition have been investigated by UV spectrum,ultraviolet second-derivative spectroscopy and fluorescence spectrum.The research results indicated that UV C irradiation make the environments of aromatic residues change according to UV spectrum and ultraviolet second-derivative spectroscopy.Stern-Volmer equation and Lineweaver-Burk equation showed that the fluorescence quenching of BSA by Pb(Ⅱ)is also a static quenching procedure and strong binding site is not change after UV C irradiation.When adding Pb(Ⅱ)to irradiated BSA,the binding constant(KS)decreased gradually;while irradiating the mixture of Pb(Ⅱ)-BSA,the binding constant(KS)increased.

Key concepts: Bovine serum albumin, Quenching (fluorescence), Chemistry, Irradiation, Ultraviolet, Ultraviolet visible spectroscopy, Fluorescence, Binding constant

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