Purification and characterization of uroporphyrinogen decarboxylase from tobacco leaves

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概要

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• 1. Uroporphyrinogen decarboxylase which catalyzes the formation of copropor-phyrinogen from uroporphyrinogen is located in the soluble fraction of tobacco leaves and was purified 72 fold through ammonium sulphate precipitation and calcium phos-phosphate gel absorption. 2. Kinetic studies indicated that the apparent Michaelis constant was 1× 10^<-6> M for uroporphyrinogen III (pH 6.5; 37℃). Uroporphyrinogen III served as a much better substrate than uroporphyrinogen I under the standard conditions of this study. 3. Enzyme activity was inhibited by thiol reagents and heavy divalent cations and was stimulated by some chelating agents. 4. Both chloride and fluoride salts inhibited the formation of coproporphyrinogen from uroporphyrinogen.

• 日本植物生理学会の論文

著者

• Miller Gene

  Huxley College Western Washington State College

• Chen Tsung

  Huxley College, Western Washington State College

• Chen Tsung

  Huxley College Western Washington State College

関連論文

• Purification and characterization of uroporphyrinogen decarboxylase from tobacco leaves

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