Literature DB >> 6812635

Affinity labeling of purified ornithine decarboxylase by alpha-difluoromethylornithine.

T Kameji, S Hayashi.   

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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Year:  1982        PMID: 6812635     DOI: 10.1016/0167-4838(82)90263-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Relationship between RNA polymerase I activity and ornithine decarboxylase in rat liver tissues.

Authors:  M Urata; N Suzuki; T Hosoya
Journal:  Biochem J       Date:  1987-01-01       Impact factor: 3.857

2.  Identical catalytic-centre activity for mouse kidney and rat liver ornithine decarboxylases as determined with antizyme and affinity labelling.

Authors:  M Marumo; S Matsufuji; Y Murakami; S Hayashi
Journal:  Biochem J       Date:  1988-02-01       Impact factor: 3.857

  2 in total

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