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• W2014039737 abstract "Escherichia coli DNA photolyase was expressed as C-terminal 6× histidine-fused protein. Purification of His-tagged E. coli DNA photolyase was developed using immobilized metal affinity chromatography with Chelating Sepharose Fast Flow. By one-step affinity chromatography, approximate 4.6 mg DNA photolyase was obtained from 400 ml E. coli culture. The purified His-tagged enzyme was combined with two chromophors, FADH and MTHF. Using the oligonucleotide containing cyclobutane pyrimidine dimer as substrate, both reversed-phase high-performance liquid chromatography and size-exclusion high-performance liquid chromatography were developed to measure the enzyme activity. The enzyme was found to be able to repair the cyclobutane pyrimidine dimer with the turnover rate of 2.4 dimers/photolyase molecule/min." @default.
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• W2014039737 date "2005-05-01" @default.
• W2014039737 modified "2023-10-16" @default.
• W2014039737 title "Activity assay of His-tagged E. coli DNA photolyase by RP-HPLC and SE-HPLC" @default.
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• W2014039737 doi "https://doi.org/10.1016/j.jbbm.2005.03.005" @default.
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