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Purification and Partial Characterization of a Peroxidase from Perilla Callus

  • Hur, Yeon-Jae (College of Natural Resources and Life Science, Dong-A University) ;
  • Lee, Han-Gil (College of Natural Resources and Life Science, Dong-A University) ;
  • Hu, Gaosheng (College of Natural Resources and Life Science, Dong-A University) ;
  • Chung, Won-Bok (College of Natural Resources and Life Science, Dong-A University) ;
  • Jeong, Soon-Jae (College of Natural Resources and Life Science, Dong-A University) ;
  • Yi, Young-Byong (College of Natural Resources and Life Science, Dong-A University) ;
  • Nam, Jae-Sung (College of Natural Resources and Life Science, Dong-A University) ;
  • Chung, Young-Soo (College of Natural Resources and Life Science, Dong-A University) ;
  • Lee, Jai-Heon (College of Natural Resources and Life Science, Dong-A University) ;
  • Kim, Doh-Hoon (College of Natural Resources and Life Science, Dong-A University)
  • Published : 2007.12.31

Abstract

Cotyledons of perilla6 were cultured on MS medium containing 0.5 mg/l NAA and 0.5 mg/l BA for 7 weeks. The activity of perilla peroxidase was observed to increase following culture stages as assessed by peroxidase assay. A peroxidase (POD) was purified from perilla tissue cultured on MS medium for 7 weeks. The peroxidase was purified using ion exchange and gel nitration chromatography. The perilla peroxidase had a molecular mass of 30 kDa by SDS-PAGE. We showed that the N-terminal amino acid sequence of this protein shared 67% identity with the tea peroxidase. As indicated by SDS-PAGE, the banding pattern of the 30 kDa polypeptide present in total soluble protein from perilla tissue was increased following culture stages. Immunoblot analysis indicated that perilla peroxidase protein appeared after 3 weeks of perilla tissue culture, and continued to increase with extended duration of tissue culture for at least 7 weeks.

Keywords

References

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