PMID:15916808: Difference between revisions

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<span style = 'font-size: large'> '''Mu, W, Zhang, D, Xu, L, Luo, Z and Wang, Y'''  (2005) Activity assay of His-tagged E. coli DNA photolyase by RP-HPLC and SE-HPLC.''J. Biochem. Biophys. Methods'' '''63''':111-24</span>
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|{{TableHeadingColor}} |'''Abstract''' || Escherichia coli DNA photolyase was expressed as C-terminal 6x 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.
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'''No author listed''' (2005) Activity assay of His-tagged E. coli DNA photolyase by RP-HPLC and SE-HPLC. ''J. Biochem. Biophys. Methods'' '''63''':111-24
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!align=left  |Abstract
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Escherichia coli DNA photolyase was expressed as C-terminal 6x 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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15916808 PubMed]
Online version:[http://dx.doi.org/10.1016/j.jbbm.2005.03.005 10.1016/j.jbbm.2005.03.005]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15916808 PubMed]
!align=left  |Keywords
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Chromatography, High Pressure Liquid/methods; Deoxyribodipyrimidine Photo-Lyase/analysis; Deoxyribodipyrimidine Photo-Lyase/isolation & purification; Deoxyribodipyrimidine Photo-Lyase/metabolism; Escherichia coli Proteins; Histidine; Kinetics; Molecular Probes; Pyrimidine Dimers/analysis; Pyrimidine Dimers/metabolism; Recombinant Fusion Proteins
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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{{LitSignificance}}

Revision as of 18:45, 1 September 2013

Citation

No author listed (2005) Activity assay of His-tagged E. coli DNA photolyase by RP-HPLC and SE-HPLC. J. Biochem. Biophys. Methods 63:111-24

Abstract

Escherichia coli DNA photolyase was expressed as C-terminal 6x 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.

Links

PubMed Online version:10.1016/j.jbbm.2005.03.005

Keywords

Chromatography, High Pressure Liquid/methods; Deoxyribodipyrimidine Photo-Lyase/analysis; Deoxyribodipyrimidine Photo-Lyase/isolation & purification; Deoxyribodipyrimidine Photo-Lyase/metabolism; Escherichia coli Proteins; Histidine; Kinetics; Molecular Probes; Pyrimidine Dimers/analysis; Pyrimidine Dimers/metabolism; Recombinant Fusion Proteins

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