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Plant and Cell Physiology, 1974, Vol. 15, No. 6 993-1005
© 1974

Article

Purification and characterization of uroporphyrinogen decarboxylase from tobacco leaves

Tsung C. Chen1 and Gene W. Miller2

Huxley College, Western Washington State College Bellingham, Washington 98225, U.S.A.

1. Uroporphyrinogen decarboxylase which catalyzes the formation of coproporphyrinogen from uroporphyrinogen is located in the soluble fraction of tobacco leaves and was purified 72 fold through ammonium sulphate precipitation and calcium phosphosphate gel absorption. 2. Kinetic studies indicated that the apparent Michaelis constant was 1 × 10-6 M for uroporphyrinogen III (pH 6.5; 37°C). 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.

1Present address: Department of Chemistry, Simon Fraser University, Burnaby 2, British Columbia, Canada.

2Present address: Biology Department, Utah State University, Logan, Utah 84322, U. S. A.

(Received June 8, 1974; )
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