Abstract
A 34-kDa cationic peroxidase (Cicpx) with a pI of 8.9 was purified to homogeneity (RZ 3.5) from the medium of cell suspension cultures of chicory ( Cichorium intybus L.) by a combination of ammonium sulphate precipitation, ultrafiltration, ion exchange and gel filtration chromatography. The partial amino acid sequence presented a low homology with other plant peroxidases. Antibody against spinach peroxidase was shown to cross react with chicory isoperoxidase on immunoblots. Unlike anionic peroxidases, Cicpx displayed a high reactivity towards guaiacol and no reactivity towards syringaldazine, indicating that Cicpx was not involved in the lignification process. Thus, further investigations are necessary to assign a specific function to this particular isoperoxidase.
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