Characterization of ornithine decarboxylase of tobacco cells and tomato ovaries.

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27 Scopus citations


Some characteristics of L-ornithine decarboxylase of tomato ovaries and tobacco cells are described. The enzyme has a pH optimum of 8.0. It requires pyridoxal phosphate and thiol reagent (dithiothreitol) for activity. It is specific for L-ornithine and has an apparent Km of 1.4 X 10-4 M. It has an apparent molecular weight of 107000. Putrescine inhibited the activity in vitro. Spermidine and spermine also inhibit the enzyme, but less effectively. It is concluded that the enzyme is similar to that of mammalian origin and likewise fulfils a function related to cell proliferation.

Original languageEnglish
Pages (from-to)373-376
Number of pages4
JournalBiochemical Journal
Issue number2
StatePublished - 1 Jan 1982

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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