Expression of a Hybrid Human Superoxide Dismutase with a High Affinity for Heparin

• 出 处: Chemical Research in Chinese Universities
• 发表日期: 2002年01期
• 关键词: heparin superoxide affinity Primer hydrophilic Sepharose clearance mutase polyac

A designed heparin-affinity of human Cu, Zn-SOD is described. The natural leader peptide of P.leiognathi Cu, Zn-SOD and a heparin-binding peptide containing a stretch of 7 Arg were fused to the N-terminal and the C-terminal of human Cu, Zn-SOD respectively. The resulted hybrid enzyme had not only a normal SOD activity but also a high affinity for heparin eluted on the heparin-Sepharose column at 0.4 mol/L NaCl. Some properties, such as the optimum pH, the thermostability and the half-life in the circulation of rats, were also analyzed.

A designed heparin-affinity of human Cu, Zn-SOD is described. The natural leader peptide of P. leiognathi Cu, Zn-SOD and a heparin-binding peptide containing a stretch of 7 Arg were fused to the N-terminal and the C -terminal of human Cu, Zn-SOD respectively. The resulting hybrid enzyme had not only a normal SOD activity but also a high affinity for heparin eluted on the heparin-Sepharose column at 0.4 mol / L NaCl. Some properties, such as optimum pH, the thermostability and the half-life in the circulation rats, were also analyzed.