Kameji T, Hayashi S
Biochim Biophys Acta. 1982 Aug 10;705(3):405-7. doi: 10.1016/0167-4838(82)90263-1.
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.
从大鼠肝脏中纯化得到的鸟氨酸脱羧酶(L-鸟氨酸羧基裂解酶,EC 4.1.1.17)用α-[5-¹⁴C]二氟甲基鸟氨酸进行亲和标记。经SDS-聚丙烯酰胺凝胶电泳分析,放射性迁移为单一主要峰,与一条Mr为50,000的单一蛋白带重合。根据结合的放射性计算表明,鸟氨酸脱羧酶有两个活性位点,每个亚基一个,纯酶的比活性应为每毫克蛋白质约1.4×10⁶ nmol CO₂/小时。