Abstract
The cell wall residue, enriched in lignin, which was obtained from non-xylem tissues of flax stems after extensive digestion with the glycanase mixture, Driselase, had appreciable peroxidase activity which was tightly bound to the wall fragments. A portion of this residual activity was solubilized by limited proteolysis using trypsin. Non-denaturing gel electrophoresis of the trypsin-solubilized extracts revealed the presence of at least one highly mobile anionic peroxidase isozyme.
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