Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824-1312.
Plant Physiol. 1992 Sep;100(1):397-402. doi: 10.1104/pp.100.1.397.
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(r) of 35,000. It has eight cysteine residues. A highly specific, high-titer antiserum to deglycosylated P8.5 was produced.
接种大麦白粉病菌(Erysiphe graminis DC.:Fr. f. sp. hordei Em. Marchal)后,观察到两种细胞外过氧化物酶增加。同工酶 P8.5 从细胞间洗涤液中通过丙酮沉淀、离子交换层析、等电聚焦和凝胶过滤进行纯化。纯化的 P8.5 是一种含有血红素的糖蛋白,Mr 为 35000。它有 8 个半胱氨酸残基。产生了针对去糖基化 P8.5 的高度特异性、高滴度抗血清。