Fielding Lee, Rutherford Samantha, Fletcher Dan
AKZO-Nobel Pharma Division, Organon Laboratories Ltd, Newhouse, Lanarkshire ML1 5SH, UK.
Magn Reson Chem. 2005 Jun;43(6):463-70. doi: 10.1002/mrc.1574.
The usefulness of bovine serum albumin (BSA) as a model protein for testing NMR methods for the study of protein-ligand interactions is discussed. Isothermal titration calorimetry established the binding affinity and stoichiometry of the specific binding site for L-tryptophan, D-tryptophan, naproxen, ibuprofen, salicylic acid and warfarin. The binding affinities of the same ligands determined by NMR methods are universally weaker (larger KD). This is because the NMR methods are susceptible to interference from additional non-specific binding. The L-tryptophan-BSA and naproxen-BSA systems were the best behaved model systems.
讨论了牛血清白蛋白（BSA）作为一种模型蛋白在测试用于研究蛋白质-配体相互作用的核磁共振方法中的实用性。等温滴定量热法确定了L-色氨酸、D-色氨酸、萘普生、布洛芬、水杨酸和华法林特异性结合位点的结合亲和力和化学计量。通过核磁共振方法测定的相同配体的结合亲和力普遍较弱（KD值较大）。这是因为核磁共振方法易受额外非特异性结合干扰的影响。L-色氨酸-BSA和萘普生-BSA系统是表现最佳的模型系统。
