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    Biochem Biophys Res Commun. 1985 Jun 28;129(3):934-42.

    Characterization of a Saponaria officinalis seed ribosome-inactivating protein: immunoreactivity and sequence homologies.

    Lappi DA, Esch FS, Barbieri L, Stirpe F, Soria M.

    A ribosome inactivating protein from Saponaria officinalis, SO-6, was purified and the N-terminus sequenced. The sequence shows extensive homology with Pokeweed antiviral protein, Pokeweed antiviral protein II, Pokeweed antiviral seed protein and dodecandrin. SDS gel electrophoresis in the Laemmli system revealed two bands of similar intensities with a smear between them, probably an artifact due to the high pI of the protein. Use of a harsher denaturing gel system resulted in one band in electrophoresis. Immune antisera was raised in rabbits against this protein and it cross reacted with other proteins (SO-5, SO-8 and SO-9) from seeds of Saponaria officinalis, but not with gelonin, Momordica charantia inhibitor and dianthin 32.

    PMID: 3925952 [PubMed - indexed for MEDLINE]

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