Institute of Genetics, University of Amsterdam, Kruislaan 318, NL-1098 SM, Amsterdam, The Netherlands.
Plant Cell Rep. 1983 Dec;2(6):304-7. doi: 10.1007/BF00270187.
A comparative study on a pure cationic and a pure anionic protein from peanut cells and petunia stem tissue respectively, both with peroxidative activity, was made. The cationic protein weighs 44 Kd and the anionic 36 Kd. No immunological cross reactivity could be detected between the two proteins. In assays for peroxidative activity using the substrates 4-aminoantipyrine, guaiacol and eugenol it was noted that the anionic protein had 1.9, 12.7, and 27.7 fold greater enzymatic activity, respectively. For overall peroxidative measurements it is suggested that aminoantipyrine is probably the superior substrate. With regard to IAA oxidase activity of the two protein fractions it was noted that the cationic enzyme possessed optimal activity at pH 3.6 and the anionic protein at pH 7.0. The latter value could only be obtained by the addition of H2O2 and dichlorophenol (DCP). Since no additives were needed for the assay of IAA oxidation by the cationic protein it is suggested that this is a true IAA oxidase while the anionic fraction is a peroxidase involved in other reactions such as lignin biosynthesis.
分别对花生细胞和矮牵牛茎组织中具有过氧化物酶活性的纯阳离子蛋白和纯阴离子蛋白进行了比较研究。阳离子蛋白的分子量为 44 kDa，阴离子蛋白的分子量为 36 kDa。两种蛋白质之间没有检测到免疫交叉反应。在用 4-氨基安替比林、愈创木酚和丁香酚作为过氧化物酶活性的底物进行的测定中，发现阴离子蛋白的酶活性分别高出 1.9、12.7 和 27.7 倍。对于总过氧化物的测量，建议使用氨基安替比林作为优选的底物。关于两种蛋白质组分的 IAA 氧化酶活性，注意到阳离子酶在 pH 3.6 时具有最佳活性，而阴离子蛋白在 pH 7.0 时具有最佳活性。后一个值只能通过添加 H2O2 和二氯苯酚（DCP）来实现。由于不需要添加任何添加剂即可测定阳离子蛋白对 IAA 的氧化作用，因此，该酶可能是一种真正的 IAA 氧化酶，而阴离子部分则是一种参与其他反应（如木质素生物合成）的过氧化物酶。
