Purification and characterization of uroporphyrinogen decarboxylase from tobacco leaves |
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Authors: | Chen Tsung C; Miller Gene W |
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Institution: | Huxley College, Western Washington State College Bellingham, Washington 98225, U.S.A. |
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Abstract: | 1. Uroporphyrinogen decarboxylase which catalyzes the formationof coproporphyrinogen from uroporphyrinogen is located in thesoluble fraction of tobacco leaves and was purified 72 foldthrough ammonium sulphate precipitation and calcium phosphosphategel absorption. 2. Kinetic studies indicated that the apparentMichaelis constant was 1 ? 10-6 M for uroporphyrinogen III (pH6.5; 37?C). Uroporphyrinogen III served as a much better substratethan uroporphyrinogen I under the standard conditions of thisstudy. 3. Enzyme activity was inhibited by thiol reagents andheavy divalent cations and was stimulated by some chelatingagents. 4. Both chloride and fluoride salts inhibited the formationof 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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