Abstract
Abstract Vanadium was found to be contaminated in commercially available Sigma Grade bovine serum albumin (BSA), fraction V. Vanadium in BSA was estimated as about 17 μg V/g protein based on the result of neutron activation analysis, and approximately 85% of the metal was easily removed by dialysis against o-phenanthroline or EDTA The levels of vanadium in Sigma Grade serum albumins from various sources were in the following order, bovine (16.7 μg V/g protein)>ovine (10.0)> rabbit (9.1)>porcine (3.9)>human (0.2). The BSA sample in 0.1 M tris-HCl buffer, pH 7.5 showed the absence of vanadyl (+4 oxidation state) ion, but when a reducing agent such as ascorbic acid or cysteine was added, an intense signal due to the presence of vanadyl ion appeared, confirming that vanadium in BSA is in the vanadate (+5 oxidation state). Furthermore, the 51V NMR spectrum of BSA at pH(D) 7.5 showed the resonance at −569.9 ppm against VOCl3 (0 ppm) as external standard in the presence of EDTA, showing that the metal ion is also present in the vanadate form. The present results point out that commercially available serum albumins should only be used after at least simple purification such as dialysis.
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