Tsutsui K, Koide N, Tomoda J, Hayashi H, Hatase O, Oda T
Acta Med Okayama. 1977 Oct;31(5):289-94.
The precipitation reaction of bovine serum albumin coupled with p-azophenylleucine with homologous antibody was inhibited by several structurally related haptens. The isobutyl group substituent on alpha-carbon atom of the leucine residue contributed more than -5.8 Kcal/mol to the free energy of binding. This value was consistent with the free energy change expected from the transfer of n-butane from an aqueous environment to liquid n-butane. The observed contribution was explained, in terms of the hydrophobic interaction of the isobutyl group with the antigen binding site of the antibody molecule. These results were also compared with other hapten-antibody systems.
牛血清白蛋白与对偶氮苯亮氨酸偶联物与同源抗体的沉淀反应受到几种结构相关半抗原的抑制。亮氨酸残基α碳原子上的异丁基取代基对结合自由能的贡献超过-5.8千卡/摩尔。该值与正丁烷从水环境转移到液态正丁烷所预期的自由能变化一致。观察到的贡献是根据异丁基与抗体分子抗原结合位点的疏水相互作用来解释的。这些结果也与其他半抗原-抗体系统进行了比较。
