CIESC Journal

• BIOTECHNOLOGY & BIOENGINEERING • 上一篇    下一篇

水蛭素聚乙二醇化及其体外抗凝活力分析

秦海娜a; 修志龙a; 张代佳a; 包永明a; 李晓晖a; 韩国柱b   

  1. a Department of Bioscience and Biotechnology, School of Environmental and Biological
    Science and Technology, Dalian University of Technology, Dalian 116024, China
    b Department of Pharmacology, Dalian Medical University, Dalian 116027, China
  • 收稿日期:1900-01-01 修回日期:1900-01-01 出版日期:2007-08-28 发布日期:2007-08-28
  • 通讯作者: 秦海娜

PEGylation of hirudin and analysis of its antithrombin activity in vitro

QIN Hainaa; XIU Zhilonga; ZHANG Daijiaa; BAO Yongminga; LI Xiaohuia; HAN Guozhub   

  1. a Department of Bioscience and Biotechnology, School of Environmental and Biological
    Science and Technology, Dalian University of Technology, Dalian 116024, China
    b Department of Pharmacology, Dalian Medical University, Dalian 116027, China
  • Received:1900-01-01 Revised:1900-01-01 Online:2007-08-28 Published:2007-08-28
  • Contact: QIN Haina

摘要: Hirudin is the most anticoagulant drug found in nature, but its short serum half-life
significantly inhibits its clinical application. The PEGylation of hirudin, the most
promising anticoagulant drug, was performed in this paper. The optimal reaction conditions
for PEGylated hirudin were investigated. When the PEGylation reaction was conducted under 4
℃ after 10h, in the borate buffer at pH 8.5, with the molar ratio 250︰1 of PEG to
hirudin, a higher modification extent was achieved. Finally, the bioactivity of PEGylated
hirudin was measured in vitro. Compared with unmodified hirudin, 26% of anti-thrombin
activity was retained.

关键词: PEGylated protein;hirudin;analysis;anti-thrombin activity

Abstract: Hirudin is the most anticoagulant drug found in nature, but its short serum half-life
significantly inhibits its clinical application. The PEGylation of hirudin, the most
promising anticoagulant drug, was performed in this paper. The optimal reaction conditions
for PEGylated hirudin were investigated. When the PEGylation reaction was conducted under 4
℃ after 10h, in the borate buffer at pH 8.5, with the molar ratio 250︰1 of PEG to
hirudin, a higher modification extent was achieved. Finally, the bioactivity of PEGylated
hirudin was measured in vitro. Compared with unmodified hirudin, 26% of anti-thrombin
activity was retained.

Key words: PEGylated protein, hirudin, analysis, anti-thrombin activity