1. Istituto di Chimica Biologica, Universitàdi Padova, Via Marzolo 3, 35131 Padova, Italy;2. Istituto di Chimica Biologica, Universitàdi Bologna, Via Irnerio 48, 40126 Bologna, Italy
Abstract:
Highly purified preparations of rat heart ornithine decarboxylase are readily phosphorylated by rat liver type-2 casein kinase-TS at the same 54 KDa protein band which is also radiolabeled by 3H-DFMO. The reaction, which is stimulated by polylysine leads to the incorporation of up to 0.8 mol P/mol ornithine decarboxylase at seryl residue(s) included in a single 8.6 KDa CNBr fragment. Partially purified preparations of ornithine decarboxylase contain a type-2 casein kinase which promotes the phosphorylation of ornithine decarboxylase at the same CNBr fragment affected by rat liver casein kinase-TS.