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  • Title: Affinity labeling of purified ornithine decarboxylase by alpha-difluoromethylornithine.
    Author: Kameji T, Hayashi S.
    Journal: Biochim Biophys Acta; 1982 Aug 10; 705(3):405-7. PubMed ID: 6812635.
    Abstract:
    Ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) purified from rat liver was affinity-labeled by alpha-[5-14C]difluoromethylornithine. On analysis by SDS-polyacrylamide gel electrophoresis, the radioactivity migrated as a single major peak that coincided with a single protein band of Mr 50,000. Calculation from bound radioactivity indicated that ornithine decarboxylase has two active sites, one for each subunit, and that pure enzyme should have a specific activity of about 1.4 x 10(6) nmol CO2/h per mg protein.
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