The adsorption of bovine serum albumin (BSA) to a chromatography resin with immobilised llama antibody fragments as affinity ligands was investigated. The maximum adsorption capacity of the affinity resin was 21.6 mg mL-1 with a Langmuir equilibrium constant of 20.4 mg mg-1. Using packed bed chromatography, BSA was adsorbed from pure BSA solutions. Recovery was achieved by desorption at pH 3. In experiments with initial BSA concentrations of 1 mg mL-1 and 0.1 mg mL-1, BSA could be concentrated to 6.9 and 7.7 mg mL-1, respectively. BSA was also isolated from filtered bovine cheese whey containing less than 0.1 mg mL-1 BSA. The purified BSA was in this case concentrated to 7.4 mg mL-1 BSA. The presence of other components in the feedstock did not alter the adsorption capacity of the affinity resin. The results show that high recovery combined with high purity can be obtained using affinity chromatography.