Maksimov I V, Cherepanova E A, Kuz'mina O I, Iarullina L G, Akhunov A A
Bioorg Khim. 2010 May-Jun;36(3):319-26. doi: 10.1134/s1068162010030039.
The chitin-binding ability of isoperoxidases isolated from 23 plants of different species was studied. The activation of peroxidases in a protein extract in the presence of this polysaccharide was found for 14 of the studied plants. Anionic isoperoxidases were shown to be sorbed on chitin and eluted from them with 1 M NaCl for 16 of the plant species. Cationic isoforms of the peroxidases of some species of the Fabaceae and Cucurbitaceae plant families also bound to chitin. An immunochemical similarity was found between the chitin-binding isoperoxidases of taxonomically distant plant species (the Pomaceous, Fabaceae, and gourd families). Moreover, a high homology of the molecular structures of the polysaccharide-binding sites was revealed for the anionic peroxidases of rice, wheat, oat, zucchini, cucumber, and radish. We propose the existence of a special class of plant peroxidases that bind with polysaccharides (chitin) and participate in the protective reactions of plants against pathogens.
对从23种不同植物中分离出的同功过氧化物酶的几丁质结合能力进行了研究。在14种被研究植物中，发现该多糖存在时蛋白质提取物中的过氧化物酶被激活。对于16种植物，阴离子同功过氧化物酶被证明可吸附在几丁质上，并用1M氯化钠从几丁质上洗脱下来。豆科和葫芦科一些植物种类的过氧化物酶阳离子同工型也与几丁质结合。在分类学上相距较远的植物种类（蔷薇科、豆科和葫芦科）的几丁质结合同功过氧化物酶之间发现了免疫化学相似性。此外，揭示了水稻、小麦、燕麦、西葫芦、黄瓜和萝卜的阴离子过氧化物酶的多糖结合位点的分子结构具有高度同源性。我们提出存在一类特殊的植物过氧化物酶，它们与多糖（几丁质）结合并参与植物对病原体的保护反应。
