Abstract
Summary Cell wall peroxidases from poplar stem were investigated through parallel biochemical and histochemical techniques. Oxidation of syringaldazine was obtained only in lignifying cells. That it was a true peroxidasic activity was demonstrated by its absolute requirement for exogeneous H 2 O 2 for in vitro assays. However syringaldazine oxidation could be obtained in situ in the absence of exogeneous hydrogen peroxide probably because of the production of H 2 O 2 by the lignifying cell walls themselves. Syringaldazine oxidase activity was strongly bound to the cell walls and fairly resistant to heat inactivation. It exhibited a very high affinity towards its substrate. The K M value was 100 to 1000 times higher with syringaldazine than with guaiacol.
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