Purification and characterization of a basic peroxidase from the medium ofcell suspension cultures of chicory

A 34-kDa cationic peroxidase (Cicpx) with a pI of 8.9 was purified to homog eneity (RZ 3.5) from the medium of cell suspension cultures of chicory (Cic horium intybus L.) by a combination of ammonium sulphate precipitation, ult rafiltration, ion exchange and gel filtration chromatography. The partial a mino acid sequence presented a low homology with other plant peroxidases. A ntibody against spinach peroxidase was shown to cross react with chicory is operoxidase on immunoblots. Unlike anionic peroxidases, Cicpx displayed a h igh reactivity towards guaiacol and no reactivity towards syringaldazine, i ndicating that Cicpx was not involved in the lignification process. Thus, f urther investigations are necessary to assign a specific function to this p articular isoperoxidase. (C) 2000 Editions scientifiques et medicales Elsev ier SAS.