Abstract
Binding of mercury to BSA and Ovalbumin was investigated by Differential Pulse Voltammetry. The method relies on the direct monitoring of peak current variation due to mercury oxidation in the presence of these two albumins. Linear calibration graphs were obtained for both BSA and Ovalbumin in concentrations ranging from 2.49 x 10 -7 to 19.6 x 10 -9 mol L -1. The acquired data was used to quantify these two proteins independently and to calculate the dissociation constants of Hg-BSA and Hg-Ovalbumin complexes.
Keywords: differential pulse voltammetry, mercury, bovine serum albumin, ovalbumin
Protein & Peptide Letters
Title: Investigations On The Binding Of Mercury Ions To Albumins Employing Differential Pulse Voltammetry
Volume: 10 Issue: 2
Author(s): Clarissa Silva Pires de Castro, Jurandir Rodrigues SouzaDe and Carlos Bloch Jr
Affiliation:
Keywords: differential pulse voltammetry, mercury, bovine serum albumin, ovalbumin
Abstract: Binding of mercury to BSA and Ovalbumin was investigated by Differential Pulse Voltammetry. The method relies on the direct monitoring of peak current variation due to mercury oxidation in the presence of these two albumins. Linear calibration graphs were obtained for both BSA and Ovalbumin in concentrations ranging from 2.49 x 10 -7 to 19.6 x 10 -9 mol L -1. The acquired data was used to quantify these two proteins independently and to calculate the dissociation constants of Hg-BSA and Hg-Ovalbumin complexes.
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Cite this article as:
Pires de Castro Silva Clarissa, SouzaDe Rodrigues Jurandir and Bloch Jr Carlos, Investigations On The Binding Of Mercury Ions To Albumins Employing Differential Pulse Voltammetry, Protein & Peptide Letters 2003; 10 (2) . https://dx.doi.org/10.2174/0929866033479059
DOI https://dx.doi.org/10.2174/0929866033479059 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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