ArticleBioMed research international2014
Efficient expression of acetylcholine-binding protein from Aplysia californica in Bac-to-Bac system.
Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Efficient Expression inMolecules (Basel, Switzerland) · 2024Article
- From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs.Frontiers in pharmacology · 2019Article
- An essential role of high-molecular-weight kininogen in endotoxemia.The Journal of experimental medicine · 2017Article
- Expression and bioactivity of human α-fetoprotein in a Bac-to-Bac system.Bioscience reports · 2017Article
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5 authors.
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Abstract
The Bac-to-Bac baculovirus expression system can efficiently produce recombinant proteins, but the system may have to be optimized to achieve high-level expression for different candidate proteins. We reported here the efficient expression of acetylcholine-binding proteins from sea hares Aplysia californica (Ac-AChBP) and a convenient method to monitor protein expression level in this expression system. Three key factors affecting expression of Ac-AChBP were optimized for maximizing the yield, which included the cell density, volume of the infecting baculovirus inoculums, and the culturing time of postinfection. We have found it to reach a high yield of ∼5 mg/L, which needs 55 h incubation after infection at the cell density of 2 × 10(6) cells/mL with an inoculum volume ratio of 1 : 100. The optimized expression system in this study was also applied for expressing another protein Ls-AChBP from Lymnaea stagnalis successfully. Therefore, this established method is helpful to produce high yields of AChBP proteins for X-ray crystallographic structural and functional studies.
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