Purfication and some properties of the nitrate reductase from Ankistrodesmus braunii

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概要

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• Purification of the nitrate reductase from Ankistrodesmus braunii to homogeneity is described. The K_m values are 0.19 mM for NO_3^-, 0.75 mM for FMNH_2, 4μM for methyl viologen, 11 μM for NADH and 30 μM for NADPH. Azide thiocyanate and nitrite inhibit the enzyme reaction competitively. Ki values for these compounds are 7.8 × 10^<-7> 1.2 × 10^<-5> and 4 × 10^<-4> M respectivelv. The molecular weight of the intact enzyme determined bv disc electrophoresis is 475,000 and that of its subunit 60,000 daltons. Difference spectra of the enzyme show the involvement of cytochrome in nitrate reduction.

• 日本植物生理学会の論文

著者

• Spiller H.

  Botanisches Institut Der Universitat

• Ahmed J.

  Botanisches Institut der Universitat

関連論文

• Purfication and some properties of the nitrate reductase from Ankistrodesmus braunii

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