Zinc ions promote the interaction between heparin and heparin cofactor II

FEBS Letters

Ragg, Hermann¹  Eckert, Ralf¹ 

[1] Department of Biotechnology, Faculty of Technology, University of Bielefeld, D-33501 Bielefeld, Germany

关键词: Serpin;    Heparin cofactor II;    Zinc;    Heparin;    Thrombin;    ATIII;    antithrombin III;    GAG(s);    glycosaminoglycan(s);    HCII;    heparin cofactor II;    RU;    response units;    SPR;    surface plasmon resonance;   

DOI  :  10.1016/S0014-5793(03)00322-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effects of bivalent cations on heparin binding, structure, and thrombin inhibition rates of heparin cofactor II were examined. Zn²⁺ – and to a lesser extent Cu²⁺ and Ni²⁺ – enhanced the interaction between heparin cofactor II and heparin as demonstrated by heparin affinity chromatography and surface plasmon resonance experiments. Metal chelate chromatography and increased intrinsic protein fluorescence in the presence of Zn²⁺ indicated that heparin cofactor II has metal ion-binding properties. The results are compatible with the hypothesis that Zn²⁺ induces a conformational change in heparin cofactor II that favors its interaction with heparin.

【 授权许可】

Unknown