Abstract
AbstractThe adsorptive stripping square‐wave voltammetric behavior of bovine serum albumin (BSA) is described. Conditions were optimized for the determination of this protein with respect to accumulation potential, accumulation time, drop size, scan rate, frequency value, and electrolyte concentration. Under these optimum conditions for the determination of BSA, two calibration plots were obtained. For an accumulation time of 60 seconds, the plot was linear in the range 0.25–1.25 μg/mL of BSA (r = 0.997); for an accumulation time of 180 seconds, the linear range was 0.10–1.25 μg/mL of BSA (r = 0.997). The square‐wave procedure offers the advantages of speed, higher sensitivity for the determination of BSA, and the discrimination against background currents. This method was applied successfully for the determination of total protein in fetal calf serum.
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