Abstract
Herein, the application of baculovirus/insect cell expres-sion system in the production of wild-type and phospha-tase active site mutant was inve stigated where Laforin proteinswere expressed in insect cells using baculovirus and comparedwith that from the E. coli expression system. The phosphataseactivities of purified recombinant Laforin against varioussubstrates such as pNPP, OMFP, and glycogen were exam-ined.In this study, the Laforin coding DNA sequence was clonedinto bacterial expression vector and expressed in E. coli.Using this construct, the polyhistidine-tagged Laforin wasalso cloned into baculoviral transfer vector pVL1393 (Fig. 1).Both plasmids have the polyh istidine tags for purificationusing a Ni-NTA resin. However, purification of polyhis-tidine-tagged Laforin was not successful using a Ni-NTAresin as previously reported by Dukhande et al.
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