Purification and Developmental Analysis of the Major Anionic Peroxidase from the Seed Coat of Glycine max

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Abstract
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.
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