Binding of gold to bovine serum albumin using flameless atomic absorption.
A graphite furnace atomic absorption spectrophotometric assay capable of accurately determining nanogram amounts of gold in biological fluids was developed. The presence of bovine serum albumin and/or phosphate in the sample reduced the method sensitivity without affecting the linear response. Binding of gold was studied by ultrafiltration using cones with a molecular weihght cutoff of 25,000. The binding of gold at various concentrations to 2 and 4% bovine serum albumin in 0.1 M phosphate buffer, pH 7.4, was independent of the gold and protein concentrations. In the 2-10 microgram/ml range, the overall binding values (mean +/- SD) of gold to 2 and 4% bovine serum albumin were 98 +/- 1.6 (n = 35) and 99 +/- 1.0% (n = 15), respectively. When ultrafiltration cones with a molecular weight cutoff of 50,000 were used, the extent of binding to 2% bovine serum albumin was 85.4 +/- 1.6% (n=11). This statistically significant difference (p less than 0.001) was due to variations in the protein retention of the two cone types. Interaction studies showed that gold was not displaced from the binding sites by salicylic acid (200 microgram/ml) or vice versa.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004347:Drug Interactions; D006046:Gold / Q000378:metabolism*; D008970:Molecular Weight; D011485:Protein Binding; D012459:Salicylates / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013054:Spectrophotometry, Atomic / Q000379:methods*
D012459:Salicylates; D012710:Serum Albumin, Bovine; D006046:Gold