Study of Binding Competition between Cu(II) and Zn(II) to Bovine Serum Albumin by Fluorescence Quenching
Hong Liang
Abstract
Hong Liang
Abstract
Fluorescence quenching of bovine serum albumin (BSA) by its interaction with Cu(Ⅱ) and Zn(Ⅱ) or with Cu(Ⅱ) alone was observed at 28℃ and physiologically pH 7.43(±0.02) applying fluorescence spectra method. The Stern-Volmer's K'sv cu.BSA, and Lineweaver-Burk's K'D CU-BSA were calculated in these two kinds of systems. The different interactions of Cu(Ⅱ) and Zn(Ⅱ) with BSA were discussed in this paper. By contrasting the single metal system with the double-metal system, the binding of Cu(Ⅱ) and BSA must be strengthened by the competition of Zn(Ⅱ).
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Fluorescence quenching of bovine serum albumin (BSA) by its interaction with Cu(Ⅱ) and Zn(Ⅱ) or with Cu(Ⅱ) alone was observed at 28℃ and physiologically pH 7.43(±0.02) applying fluorescence spectra method. The Stern-Volmer's K'sv cu.BSA, and Lineweaver-Burk's K'D CU-BSA were calculated in these two kinds of systems. The different interactions of Cu(Ⅱ) and Zn(Ⅱ) with BSA were discussed in this paper. By contrasting the single metal system with the double-metal system, the binding of Cu(Ⅱ) and BSA must be strengthened by the competition of Zn(Ⅱ).
Key concepts: Bovine serum albumin, Chemistry, Quenching (fluorescence), Fluorescence, Metal, Zinc, Copper, Analytical Chemistry (journal)