Purification and Partial Characterization of a Peroxidase from Perilla Callus
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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 filtration 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.
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 filtration 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.