Purification and Characterization of Molecular and Immunological Properties of Rice Ferredoxin-Nitrite Reductase(Biological Chemistry)

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概要

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• Ferredoxin-nitrite reductase [EC 1.7.7.1] has been purified to apparent homogeneity from rice (Oryza sativa cv. Kinmaze) leaves by a procedure used for the spinach enzyme [S. Ida and B. Mikami, Biochim. Biophys. Acta, 681, 167 (1986)]. The rice enzyme consists of a single polypeptide of molecular weight of 60,000 with 536 amino acid residues. The enzyme showed nearly identical absorption, circular dichroism, and magnetic circular dichroism spectra to those of the spinach enzyme, indicating the presence of the same prosthetic groups and protein conformation in both enzymes. The apparent Km values for nitrite and methyl viologen were 360μM and 63 μM, respectively. The pH optimum was 7.6. These kinetic parameters are indistinguishable from those reported for spinach nitrite reductase. Monospecific antiserum against purified rice enzyme cross-reacted with nitrite reductases from a variety of higher plants and some phylogenetically divergent plants. Immunological comparisons indicated the rice enzyme is much more closely related to the other monocot enzymes in antigenic structure than to the dicot enzyme proteins. The results lend further support to our previous study [S. Ida, Plant Sci., 49, 111 (1987)] that spinach ferredoxin-nitrite reductase is serologically more related to the dicot enzymes than to the monocot nitrite reductases. Conspicuous differences between the rice and spinach enzymes were found in their molecular sizes and antigenicity. Relatedness of amino acid compositions of the enzyme proteins is discussed in relation to antigenic properties of ferredoxin-nitrite reductase.

• 社団法人日本農芸化学会の論文
• 1989-10-23

著者

• Ida Shoji

  The Research Institute For Food Science Kyoto University

• Iwagami Kazuki

  The Research Institute For Food Science Kyoto University

• MINOBE Shinji

  The Research Institute for Food Science, Kyoto University

• Minobe Shinji

  The Research Institute For Food Science Kyoto University

関連論文

• Purification and general properties of spinach leaf nitrite reductase
• Purification of Nitrate Reductase by Methyl Viologen-bound CMSephadex C-50 from a Cyanobacterium, Plectonema boryanum
• Reversible Inactivation of Ferredoxin-Nitrate Reductase from the Cyanobacterium Plectonema boryanum. The Role of Superoxide Anion and Cyanide
• Purification and Characterization of Assimilatory Nitrate Reductase from the Cyanobacterium Plectonema boryanum
• Isolation and characterization of NADH-glutamate synthase from pea (Pisum sativum L.)
• Purification and Characterization of Molecular and Immunological Properties of Rice Ferredoxin-Nitrite Reductase(Biological Chemistry)
• Biosynthesis of Ferredoxin-Nitrite Reductase in Rice Seedlings
• Glutamate synthase in developing pea cotyledons : Occurrence of NADH-dependent and ferredoxin-dependent enzymes
• Corn leaf glutamate synthase : Purification and properties of the enzyme
• The Isolation of Multiple Forms and Product Specificity of Rice Lipoxygenase

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