Ito H, Hiraoka N, Ohbayashi A, Ohashi Y
Bioproducts Development Center, Takara Shuzo Co., Ltd., Shiga, Japan.
Agric Biol Chem. 1991 Oct;55(10):2445-54.
Four peroxidase components, named RP-2, 4, 6, and 7, were isolated from rice (Oryza sativa L.) green leaves. Isoelectric focusing indicated that each preparation was homogeneous. The molecular weights of RP-2, 4, 6, and 7 estimated by SDS-PAGE were 48,000, 48,000, 40,000, and 39,500, and their isoelectric points were 5.4, 8.1, 9.3, and 9.2, respectively. The activity of every preparation was maximum around pH 5.0. Antisera against these purified enzymes were raised in rabbits. Ouchterlony double diffusion tests with these antisera suggested that RP-6 and 7 were immunochemically identical and RP-2 and 4 were identical in parts and that RP-6 and 7 were quite different from RP-2 and 4. Analysis of the N-terminal amino acid sequences also showed that these peroxidase components were classified into two groups. The polymerase chain reaction showed that RP-2 and/or RP-4 contained an active central region, which is homologous to other plant peroxidases.
从水稻（Oryza sativa L.）绿叶中分离出四种过氧化物酶组分，分别命名为RP - 2、4、6和7。等电聚焦表明每种制剂均为纯品。通过SDS - PAGE估计，RP - 2、4、6和7的分子量分别为48,000、48,000、40,000和39,500，其等电点分别为5.4、8.1、9.3和9.2。每种制剂的活性在pH 5.0左右最高。用这些纯化酶在兔体内制备抗血清。用这些抗血清进行的欧氏双扩散试验表明，RP - 6和7在免疫化学上相同，RP - 2和4部分相同，且RP - 6和7与RP - 2和4有很大差异。对N端氨基酸序列的分析也表明，这些过氧化物酶组分可分为两组。聚合酶链反应表明，RP - 2和/或RP - 4含有一个与其他植物过氧化物酶同源的活性中心区域。
