Expression of Bovine Lactoferrin C-lobe in Rhodococcus erythropolis and Its Purification and Characterization
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概要
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A Rhodococcus erythropolis expression system for the bovine lactoferrin C-lobe was constructed. The DNA fragments encoding the BLF C-lobe were amplified and cloned into vector pTip LCH1.2. R. erythropolis carrying the pTip-C-lobe was cultured at 30 °C with shaking, and expression of the rBLF C-lobe was induced by adding 1 μg/ml (final concentration) thiostrepton. The rBLF C-lobe was isolated in native and denatured (8 M urea) form by Ni-NTA affinity chromatography. To obtain a bioactive rBLF C-lobe, the protein isolated in the denatured form was refolded by stepwise dialysis against refolding buffers. The antibacterial activity of the rBLF C-lobe was tested by the filter-disc plate assay method. The refolded rBLF C-lobe demonstrated antibacterial activity against selected strains of Escherichia coli.
- 2006-11-23
著者
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Shimazaki Kei-ichi
Dairy Science Laboratory Graduate School Of Agriculture Hokkaido University
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KIM Woan-Sub
Dairy Food Science Laboratory, Research Faculty of Agriculture, Hokkaido University
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Shimazaki Kei-ichi
Dairy Chemistry Research Laboratory Department Of Bioindustrial Chemistry Division Of Bioresource Ch
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Kim Woan-sub
Dairy Science Laboratory Graduate School Of Agriculture Hokkaido University
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Tamura Tomohiro
Molecular Environmental Microbiology Laboratory Graduate School Of Agriculture Hokkaido University
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SHIMAZAKI Kei-ichi
Dairy Chemistry Laboratory, Department of Animal Science, Obihiro University of Agriculture and Veterinary Medicine
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