| Literature DB >> 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.Entities:
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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