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Purification of NAD glycohydrolase from Agkistrodon acutus venom
Shuang Ding Wu1, Yanli Liu, Xiaolong Xu
1Laboratory of Internal Friction and Defects in Solids, Institute of Solid State Physics, Chinese Academy of Sciences, Hefei 230031, China. sdwu@mail.iisp.ac.cn
Protein Expression and Purification
|July 24, 2002
Abstract:
NAD glycohydrolase (NADase) from Agkistrodon acutus venom was purified to electrophoretic homogeneity by a fast, reproducible 3-step procedure including Q Sepharose Fast Flow, Superdex 75, and Mono S column chromatography. This new procedure gave a 15.6-fold purification with a recovery yield of 7.9% and a specific activity of 12.8 units/mg.
