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Purification and characterization of an antiviral ribosome-inactivating protein from Chenopodium album L



Purification and characterization of an antiviral ribosome-inactivating protein from Chenopodium album L



Agricultural Chemistry & Biotechnology 43(3): 125-130



An antiviral protein (CAP30) with ribosome-inactivating activity was purified from the leaves of Chenopodium album L. through ammonium sulfate precipitation and column chromatography using S-Sepharose, Blue-Sepharose, FPLC Suprose12 HR, and FPLC Mono-S. The molecular weight of CAP30 was estimated to be 30 kD. CAP30 was thermostable, maintaining its activity even after incubation at 70degreeC for 30 min, and was stable in the pH range of 6 to 9. In a cell-free in vitro translation system using rabbit reticulocyte lysate, protein synthesis was inhibited by the addition of CAP30 with an IC50 of 2.26 pM. The comparison of N-terminal amino acid sequences of this protein with the known ribosome-inactivating proteins (RIPs) revealed that it had some sequence homology with PAP-S and PAP-R from pokeweed (Phytolacca americana) and dodecandrin from P. dodecandra, but had no sequence homology with RIPs from other plants belonging to different orders. The mosaic symptoms on tobacco leaves caused by cucumber mosaic virus infection was completely inhibited by 100 ng/ml of the pure CAP30 protein.

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Accession: 011226619

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