Abstract
Phytolacca dodecandra (L'Herit) grown in cell cultures was investigated for content of ribosome-inhibiting
proteins, which was evaluated by measuring inhibition of protein synthesis in a cell-free
rat liver extract. Calli initiated from leaf, cotyledon, radicle, and hypocotyl and
suspension cells initiated from leaf and cotyledon exhibited protein synthesis-inhibiting
activity. Ribosome-inhibiting proteins were purified at least 14 times from suspension
cells of P. dodecandra. The purified protein fraction contained two proteins as seen by sodium dodecyl sulphate
polyacrylamide gel electrophoresis. The relative molecular masses were 30,000 and
31,000 and they showed a pI > 9.3. These new RIP's were shown to be different from
dodecandrin with respect to molecular mass.
Key words
Phytolacca dodecandra
- ribosome-inhibiting protein - biological test systems - protein purification
