Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Purification and Characterization of Peroxidases Correlated with Lignification in Poplar Xylem1

Jørgen Holst Christensen, Guy Bauw, Karen Gjesing Welinder, Marc Van Montagu*, and Wout Boerjan

Laboratorium voor Genetica, Departement Genetica, Vlaams Interuniversitair Instituut voor Biotechnologie, Universiteit Gent, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium (J.H.C., G.B., M.V.M., W.B.); and Department of Protein Chemistry, University of Copenhagen, DK-1353 København K, Denmark (K.G.W.)

Lignin is an integral cell wall component of all vascular plants. Peroxidases are widely believed to catalyze the last enzymatic step in the biosynthesis of lignin, the dehydrogenation of the p-coumaryl alcohols. As the first stage in identifying lignin-specific peroxidase isoenzymes, the classical anionic peroxidases found in the xylem of poplar (Populus trichocarpa Trichobel) were purified and characterized. Five different poplar xylem peroxidases (PXP 1, PXP 2, PXP 3-4, PXP 5, and PXP 6) were isolated. All five peroxidases were strongly glycosylated (3.6% to 4.9% N-glucosamine), with apparent molecular masses between 46 and 54 kD and pI values between pH 3.1 and 3.8. Two of the five isolated peroxidases (PXP 3-4 and PXP 5) could oxidize the lignin monomer analog syringaldazine, an activity previously correlated with lignification in poplar. Because these isoenzymes were specifically or preferentially expressed in xylem, PXP 3-4 and PXP 5 are suggested to be involved in lignin polymerization.

1   This research was supported by funds from the Danish Agricultural and Veterinary Research Council, the European Commission (AIR2-CT93-1661), and Novo Nordisk (Denmark).
*   Corresponding author; e-mail mamon{at}gengenp.rug.ac.be; fax 32-9-264-5349.

Plant Physiol. (1998) 118: 125-135
Copyright Clearance Center:   0032-0889/98/118//11
© 1998 American Society of Plant Physiologists




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