Bodinierin, one of the major proteins in the kernels of camphor tree (Cinnamomum Bodinieri), has been identified as a novel type II ribosome-inactivating protein. Using sepharose-4B column chromatography followed by acid precipitation and ammonium sulfate precipitation, bodinierin has been purified to be homogeneous as characterized by SDS-PAGE. Bodinierin was composed of two chains (A- and B-chain) with the molecular weight of 31 and 34 kDa respectively. The reduced bodinierin showed strong inhibitory activity to protein synthesis in the rabbit reticulocyte lysate and the RNA N-glycosidase activity. The bodinierin also displayed the carbohydrate binding activity to agglutinate rabbit erythrocyte. A comparison of bodinierin with cinnamomin and porrectin that were isolated from the kernels of other species of the same genus (Cinnamomum) demonstrated that they had similar structure and biological activities, which provided phylogenetic evidence to the three species.
Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.