Loun B, Hage D S
Department of Chemistry, University of Nebraska, Lincoln 68588-0304, USA.
J Chromatogr B Biomed Appl. 1995 Mar 24;665(2):303-14. doi: 10.1016/0378-4347(94)00547-i.
High-performance affinity chromatography was used to examine the binding of thyroid hormones and related compounds at the warfarin and indole sites of human serum albumin (HSA). This was studied by continuously applying L-triiodothyronine (L-T3), L-reverse triiodothyronine (L-rT3) or structural analogs of these compounds to an immobilized HSA column while making injections of site-specific probe molecules (i.e. R-warfarin and L-tryptophan). The results were compared with those obtained previously for L-thyroxine (L-T4). Equilibrium association constants and thermodynamic parameters measured by this approach showed good agreement with previous models reported for L-T4 and L-T3 at their high-affinity sites on HSA. This data confirmed that the phenol groups of L-T4 and L-T3 played a significant role in the binding of these compounds at the indole site. Work performed at the warfarin site and with other solutes (e.g. L-rT3) indicated that additional factors, such as interactions through the thyronine backbone or terminal amine and carboxyl groups of these compounds, could also be involved in the binding of thyroid hormones to HSA.
采用高效亲和色谱法研究甲状腺激素及相关化合物与人血清白蛋白（HSA）华法林位点和吲哚位点的结合情况。通过将L-三碘甲状腺原氨酸（L-T3）、L-反式三碘甲状腺原氨酸（L-rT3）或这些化合物的结构类似物连续施加到固定化HSA柱上，同时注射位点特异性探针分子（即R-华法林和L-色氨酸）来进行此项研究。将结果与先前获得的L-甲状腺素（L-T4）的结果进行比较。用这种方法测得的平衡缔合常数和热力学参数与先前报道的L-T4和L-T3在HSA上高亲和力位点的模型结果吻合良好。该数据证实L-T4和L-T3的酚基在这些化合物与吲哚位点的结合中起重要作用。在华法林位点及与其他溶质（如L-rT3）进行的研究表明，这些化合物通过甲状腺素主链或末端胺基和羧基的相互作用等其他因素也可能参与甲状腺激素与HSA的结合。
