Models for studying the binding capacity of albumin to zinc by stripping voltammetry

✍ Scribed by Juan C. Vidal; Gemma Cepria; Juan R. Castillo

• Publisher: Elsevier Science
• Year: 1992
• Tongue: English
• Weight: 922 KB
• Volume: 259
• Category: Article
• ISSN: 0003-2670
• DOI: 10.1016/0003-2670(92)85085-k

✦ Synopsis

The complexatlon capacity of albumin to zmc was studied by different voltammetrlc methods Cycbc voltammetry was used with a hanging mercury drop electrode (HMDE) to diagnose quahtatlvely the electrode mechanisms occumng at a mercury electrode and to evaluate the charge-transfer rate constant of the electrochemical reactlon of zmc m the presence of different concentrations of albumin The condltlonal stability constant of the zinc-albumin complex was determined pseudo-polarographlcally by differential-pulse anodlc strlppmg voltammetry (DP-ASV) with a Nafion-coated mercury film electrode (Nf-MFE) This electrode permits the determmatmn of free (labde) zmc and rejection of the mterfenng adsorption of free albumin on the glassy carbon surface A mean conditional stability constant of log p' = 6 10 k 0 16 was obtained by this method DP-ASV was used to calculate p' by titrating an albumin solution wnth Zn(II) and by Ruzlc data treatment In this instance a mean of log /3' = 5 49 + 0 28 was found with the HMDE and Nf-MFE The results are compared and discussed