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Adsorption of Ribonuclease A and Lysozyme at the Mercury/Solution Interface

✍ Scribed by Jasmina Vidić; Desanka Sužnjević; Milenko Erceg; Dušan Vučelić

Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
59 KB
Volume
61
Category
Article
ISSN
0026-265X

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✦ Synopsis

The adsorption of lysozyme and RNase A at a dropping mercury electrode from 0.1 M Tris-HCl ϩ 1 mM EDTA ϩ 0.2 M KCl buffer solution (pH 8.8) was investigated by applying phase-sensitive alternating current polarography. Both proteins are strongly adsorbed over a wide range of electrode potential around the zero charge potential. The adsorption of the protein resulted in a decrease in the double-layer capacitance component to the capacitance of the supporting electrolyte/mercury double layer. Changes in capacitance allowed Frumkin adsorption isotherms and thermodynamic adsorption parameters to be obtained. Apart from the capacity current components, the faradaic current components were also monitored to test the accessibility of protein -S-S-bonds to redox processes at the mercury surface.

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