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Zoological Research
Kunming Institute of Zoology, Chinese Academy of Sciences
ISSN: 2095-8137
Vol. 29, No. 4, 2008, pp. 399-404
Bioline Code: zr08061
Full paper language: Chinese
Document type: Research Article
Document available free of charge

Zoological Research, Vol. 29, No. 4, 2008, pp. 399-404

 en Purification and Characterization of 5'-nucleotidase from Trimeresurus albolabris check for this species in other resources Venom
CHEN, Xia; YU, Xiao-dong; DENG, Min; LI, Hui; HE, Qi-yi & LIU, Jian-ping


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.

Trimeresurus albolabris; Snake venom; 5'-nucleotidase; Isolation and purification

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