Volume 29 Issue 4
Jul.  2008
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CHEN Xia, YU Xiao-dong, DENG Min, LI Hui, LIN Yi-xin, HE Qi-yi, LIU Jian-ping. Purification and Characterization of 5′-nucleotidase from Trimeresurus albolabris Venom. Zoological Research, 2008, 29(4): 399-404. doi: 10.3724/SP.J.1141.2008.04399
Citation: CHEN Xia, YU Xiao-dong, DENG Min, LI Hui, LIN Yi-xin, HE Qi-yi, LIU Jian-ping. Purification and Characterization of 5′-nucleotidase from Trimeresurus albolabris Venom. Zoological Research, 2008, 29(4): 399-404. doi: 10.3724/SP.J.1141.2008.04399

Purification and Characterization of 5′-nucleotidase from Trimeresurus albolabris Venom

doi: 10.3724/SP.J.1141.2008.04399
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  • Corresponding author: YU Xiao-dong
  • Received Date: 2008-01-30
  • Rev Recd Date: 1900-01-01
  • Publish Date: 2008-08-22
  • A 5′-nucleotidase was isolated and purified from the snake venom of T. albolabris using three steps of chromatography including DEAE-SephadexA-25, Sephadex-G-100 and CM-Sephadex C-50. Using SDS-PAGE and HPLC column chromatography the purified 5′-nucleotidase proved to be homogenous. It was a glycoprotein with a molecular weight of 48.03 kDa. The enzymatic activities of the purified 5′-nucleotidase were 330.33 µg Pi/min mg and 123.56 µg Pi/min mg when using AMP(adenosine monophosphate) and ADP(adenosine diphosphate) as substrates, respectively. Metal ions, including Zn2+, Fe3+ and Cu2+, could inhibit 5′-nucleotidase activity, as did EDTA. Its optimum pH was nine and its optimum temperature was 50°C. It has a potent inhibitory effect on rabbit platelet aggregation induced by ADP.
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