Investigations on the binding of mercury ions to albumins employing differential pulse voltammetry.
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(-9) 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.
Castro
Clarissa Silva Pires de
CS
Laboratório de Espectrometria de Massa, Embrapa Recursos Genéticos e Biotecnologia, P O Box 02372, 70.770-900, Brasília-DF, BRAZIL.
SouzaDe
Jurandir Rodrigues
JR
Bloch
Carlos
C
D000418:Albumins / Q000032:analysis / Q000378:metabolism*; D007700:Kinetics; D008628:Mercury / Q000378:metabolism*
D000418:Albumins; D008628:Mercury