Modification of a reaction vessel for the determination of total mercury in hair by cold vapor atomic absorption spectrometry.

A classical cold vapor atomic absorption spectrometric (CVAAS) method for the determination of total mercury in blood has been previously adapted for application to samples of human hair. The reaction vessel specified in the original adaptation was, however, large and difficult to use with small hair samples. In the present study, the reaction vessel has been modified and reduced in size and the protocols have been optimized in order to provide an analytical method that is more efficient, less time-consuming, and gives lower blank values than the original adaptation. The optimized method was validated by multiple, independent, replicated assays of certified reference hair samples, and the mean recovery obtained (98.7%) indicated an efficient performance of the digestion and detection processes. The method was applied to the assay of 144 hair samples derived from populations that had or had not been exposed to mercury from environmental sources. The results from all of the samples analyzed were consistent with those published previously for similar samples.

Determination of Se(IV) by anodic stripping voltammetry using gold electrodes made from recordable CDs.

This work presents a simple, reproducible and low cost method, employing differential pulse anodic stripping voltammetry, for determination of selenium(IV). A gold electrode obtained from recordable compact disks (CD-R) was used to evaluate the voltammetric behavior of the metallic ion in 0.1molL(-1) HClO(4). To evaluate the voltammetric behavior of Se(IV), parameters such as deposition potential and deposition time were optimized. A wide linear response range, from 0.5 to 291ngmL(-1), was obtained using a 5.0mm diameter gold electrode. Recovery tests for Se(IV) utilizing standard reference solutions provided values between 94 and 96%.

The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide. A voltammetric study.

Binding of zinc to a 19 mer double-stranded oligodeoxyribonucleotide was investigated by anodic stripping voltammetry and cyclic voltammetry in order to understand the roles of zinc in DNA cleavage catalyzed by mung bean nuclease. These methods rely on the direct monitoring of zinc oxidation current in the absence and in the presence of the oligo. Zinc titration curves with the ds-oligodeoxyribonucleotide were obtained in concentrations ranging from 3.62 x 10(-9) to 3.62 x 10(-8) M and 4.06 x 10(-10) to 5.25 x 10(-9) M. The acquired data were used to determine the dissociation constant, stoichiometry and zinc binding sites of the complex and to understand the specific changes of ds-oligodeoxyribonucleotide secondary structure by zinc binding. The oxidation-reduction process of zinc was also investigated by cyclic voltammetry through I (oxidation current) versus v(1/2) (square root of scan rate) curves in the absence and in the presence of the double-stranded oligodeoxyribonucleotide.

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.