Ascorbate peroxidase (EC 1.11.1.11), a heme-containing homodimeric protein, is a hydrogen peroxide-scavenging enzyme, playing an important role in plants in order to protect them from oxidative stress, thus adverting cellular damage. Several ascorbate peroxidase isoenzymes have been reported but the
A highly specific rabbit antiserum raised against peroxidase (PRXa) from petunia (Petunia hybrida) was used to investigate the antigenic relatedness of peroxidases in the Solanaceae. After SDS-PAGE of crude leaf extracts from a large number of species of this family, immunoblotting revealed that
The enzyme peroxidase was isolated from the leaves of the tobacco plant Xanthi (intact and infected with weakly (XY) and highly (XT) pathogenic strains of potato X-virus) and partially purified. The original extract (the 30,000 g supernatant) was purified by ammonium sulfate at 30--80% of saturation
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