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Issue:ISSN 1000-7083
          CN 51-1193/Q
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Your Position :Home->Past Journals Catalog->2009 Vol.28 No.1

Construction, Expression and Purification of S-Adenosylhomocysteine Hydrolase from Amphioxus Branchiostoma belcheri tsingtaunese
Author of the article:WANG Yuan, ZHAO Bo-sheng*
Author's Workplace:(School of Life Sciences, Shandong University of Technology, Zibo, Shandong Province 255049, China)
Key Words: Branchiostoma belcheri tsingtaunese; S-Adenosylhomocysteine hydrolase; gene expression; purification
Abstract:S-Adenosylhomocysteine hydrolase gene of amphioxus Branchiostoma belcheri tsingtaunese was induced to express the fusion protein in E. coli. Amphioxus SAHH gene was cloned into a bacterial expression vector pGEX-6P-1 and the recombinant plasmid pGEX-6P-1-SAHH was transferred into E. coli JM109. The GST-SAHH was induced by IPTG, and the fusion protein was purified by affinity purification. The molecular mass of fusion protein GST-SAHH was estimated to be approximately 70 kDa by SDS-PAGE electrophoresis. A prokaryotic expression plasmid containing amphioxus SAHH gene was successfully constructed, and it could be effectively purified by the GST affinity column.
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