锌与人类血清白蛋白的结合：两个结合位点的证据

Zinc-human serum albumin association: testimony of two binding sites.

作者信息

André C, Guillaume Y C

机构信息

Laboratoire de Chimie Analytique, Faculté de Medecine-Pharmacie, Equipe des Sciences Séparatives et Biopharmaceutiques (2SB), Place Saint Jacques, 25030 Besançon Cedex, France.

出版信息

Talanta. 2004 May 28;63(2):503-8. doi: 10.1016/j.talanta.2003.10.054.

DOI:10.1016/j.talanta.2003.10.054

PMID:18969460

Abstract

The zinc cation (Zn(2+)) binding to human serum albumin (HSA) was studied using a non-equilibrium approach in order to prove two HSA binding sites. The effect of the bulk solvent pH and column temperature T on this binding and the corresponding thermodynamic data were also investigated. It appeared that the association process can be divided into two pH value ranges due to a predominant Zn(2+) interaction with either HSA site I or site II. It was also demonstrated that the Zn(2+) affinity for the site II was weakly affected by modifying the mobile phase pH whereas for the site I, the affinity constant increased strongly with increasing the pH of the bulk solvent.

摘要

为了证明人血清白蛋白（HSA）存在两个结合位点，采用非平衡方法研究了锌阳离子（Zn(2+)）与人血清白蛋白（HSA）的结合。还研究了本体溶剂pH值和柱温T对这种结合的影响以及相应的热力学数据。结果表明，由于Zn(2+)与HSA的位点I或位点II存在主要相互作用，缔合过程可分为两个pH值范围。还证明了改变流动相pH值对Zn(2+)与位点II的亲和力影响较弱，而对于位点I，随着本体溶剂pH值的升高，亲和常数显著增加。