Characteristics and Physiological Function of NADP-Malic Enzyme from Wheat
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概要
- 論文の詳細を見る
Kinetic and structural properties of NADP-malic enzyme (NADP-ME, EC 1.1.1.40) purified from stems and roots of wheat (Triticum aestivum), along with the possible physiological role of the enzyme were examined. Enzyme purification from stems sequentially involved precipitation with crystalline ammonium sulfate, anion-exchange, affinity and size exclusion chromatographies, while anion-exchange chromatography was omitted for the enzyme purification from roots. SDS-PAGE of the purified enzyme showed a single protein band with a molecular mass of 72-kDa. Enzyme activity was dependent on the presence of a bivalent metal cation, Mg^<2+> or Mn^<2+>. Binding characteristics of each metal ion suggest the existence of at least two different binding sites with distinct affinities. Nonetheless, activity response to NADP^+ and L-malate exhibited Michaelis-Menten behavior with K_m values of 37 and 960 μM, respectively. The amount and activity of NADP-ME were increased by GSH, cellulase and macerozyme. From these results we suggest that NADP-ME of wheat could be implicated in defense-related deposition of a.
- 日本植物生理学会の論文
著者
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Andreo Carlos
Centro De Estudios Fotosinteticos Y Bioquimicos Facultad De Ciencias Bioquimicas Y Farmaceuticas
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Spampinato Claudia
Centro De Estudios Fotosinteticos Y Bioqufmicos Universidad Nacional De Rosario
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Casati P
Univ. Nacional De Rosario Rosario Arg
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Casati Paula
Centro De Estudios Fotosinteticos Y Bioquimicos Universidad Nacional De Rosario
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Andreo Carlos
Centro De Estudios Fotosinteticos Y Bioquimicos (cefobi) Universidad Nacional De Rosario
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Casati Paula
Centro de Estudios Fotosinteticos y Bioqufmicos, Universidad Nacional de Rosario
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