Abstract
A novel, type-1 ribosome-inactivating protein (RIP), abelesculin, from the mature seeds of Abelmoschus esculentus was successively purified to homogeneity using ammonium sulfate precipitation, ion-exchange chromatography and size-exclusion chromatography. Abelesculin was found to have a molecular mass of 30 kDa and a pI of more than 10.1. The protein depurinates 28S rRNA in the ribosomes of rat liver with an EC50 (concentration causing 50% cleavage) of 62.8 pM. Study of the sequence of the 26 N-terminal amino acids of the protein revealed a close relationship with other RIPs. This study reports for the first time that RIPs exist in Malvaceae plants.
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