SOLUBILIZATION OF WALL-BOUND PEROXIDASES BY LIMITED PROTEOLYSIS

The cell wall residue, enriched in lignin, which was obtained from non -xylem tissues of flax stems a er extensive digestion with the glycana se mixture, Driselase, had appreciable peroxidase activity which was t ightly bound to the wall fragments. A portion of this residual activit y 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.