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