Department of Biological Sciences, Bowling Green State University, Bowling Green, Ohio 43403.
Plant Physiol. 1991 May;96(1):214-20. doi: 10.1104/pp.96.1.214.
We show that the majority of peroxidase activity in soybean (Glycine max var Williams 82) seeds is localized to the seed coat. A single isozyme is responsible for this activity and has been purified to electrophoretic homogeneity by successive chromatography on DEAE Sepharose Fast Flow, concanavalin A-Sepharose, and Sephadex G-75. The peroxidase exhibits a pl of 4.1, an apparent molecular mass of 37 kilodaltons, and has properties characteristic of a glycoprotein. The enzyme begins to accumulate approximately 21 days after anthesis and continues to do so throughout the maturation of the seed coat where it can represent at least 5% of the soluble protein in dry seed coats. Due to its localization in the seed, we propose that this isozyme may play a role in the hardening of the seed coat.
我们表明，大豆（Glycine max var Williams 82）种子中的大多数过氧化物酶活性都定位于种皮中。一种同工酶负责这种活性，并且已经通过在 DEAE Sepharose Fast Flow、伴刀豆球蛋白 A-Sepharose 和 Sephadex G-75 上连续层析，电泳纯化为单一组分。该过氧化物酶的等电点为 4.1，表观分子量为 37 千道尔顿，具有糖蛋白的特性。该酶在授粉后约 21 天开始积累，并在种皮成熟过程中持续积累，在干燥的种皮中，它至少可以代表可溶性蛋白的 5%。由于其在种子中的定位，我们推测该同工酶可能在种皮硬化过程中发挥作用。
