Increases in two extracellular peroxidases were observed following inoculation of barley (Hordeum vulgare L.) with the powdery mildew pathogen (Erysiphe graminis DC.: Fr. f. sp. hordei Em. Marchal). The more prominent isozyme, P8.5, was purified from intercellular wash fluids by acetone precipitation, ion-exchange chromatography, isoelectric focusing, and gel filtration. Purified P8.5 is a heme-containing, glycoprotein with a M, of 35,000. It has eight cysteine residues. A highly specific, high-titer antiserum to deglycosylated P8.5 was produced.f. sp. hordei, the causal agent of powdery mildew of barley, results in a 16-fold increase in extracellular peroxidase activity within 3 d of inoculation. The increased activity is a consequence of an increase in two isozymes with pI values of 8.5 and 5.2, which we have named P8.5 and P5.2, respectively (11).Our long-term goal is to test the hypothesis that the pI 8.5 and pl 5.2 peroxidase isozymes are involved in the deposition of lignin-like compounds in papillae and in cross-linking phenolic or phenylpropanoid compounds into preexisting cell-wall polymers. As a step toward this goal, we report the purification of P8.5.Peroxidase isozymes, which are induced following inoculation with pathogens, are thought to be involved in the deposition of lignin-like compounds at sites of attempted penetration and wounding (6). The lignin-like deposits are