Purification and Characterization of Rice Peroxidases(Biological Chemistry)
スポンサーリンク
概要
- 論文の詳細を見る
Four peroxidase components, named RP-2, 4, 6, and 7, were isolated from rice (Oryza saliva 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.
- 社団法人日本農芸化学会の論文
- 1991-10-23
著者
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Hiraoka Nobutsugu
Bioproducts Development Center Takara Shuzo Co. Ltd.
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Ohashi Yuko
Department Of Molecular Biology National Institute Of Agrobiological Resources
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ITO Hiroyuki
Bioproducts Development Center, Takara Shuzo Co., Ltd.
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OHBAYASHI Akira
Central Research Laboratories, Takara Shuzo Co., Ltd.
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Ohbayashi Akira
Central Research Laboratories Takara Shuzo Co. Ltd.
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Ito Hiroyuki
Bioproducts Development Center Takara Shuzo Co. Ltd.
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