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- W1552152044 abstract "A novel type 2 ribosome-inactivating protein (RIP) that we named ebulin 1 has been isolated from leaves of Sambucus ebulus L. (Caprifoliaceae). In vitro ebulin 1 strongly inhibited protein synthesis by rabbit reticulocyte lysates, rat brain, and rat liver cell-free systems but did not affect in vitro plant nor bacterial protein synthesis. Ebulin 1 is composed of two subunits, a catalytic A subunit (M(r) 26,000) and a D-galactose-binding lectin B subunit (M(r) 30,000). Amino-terminal amino acid sequence homology revealed the novelty that the ebulin 1 A-chain shares a high degree of homology not with the A-chain of other type 2 RIPs but rather with the Cucurbitaceae type 1 RIP briodin S and the anti-human immunodeficiency virus type I proteins trichosanthin and TAP 29. Upon treatment with acid aniline the rRNA from ebulin 1-treated rabbit reticulocyte ribosomes released the RNA fragment which is diagnostic of RIP catalytic action. Ebulin 1 was nontoxic to mice up to 2 mg/kg of body weight and did not inhibit protein synthesis in cultured NHC human epithelial cells which are highly sensitive to ricin." @default.
- W1552152044 created "2016-06-24" @default.
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- W1552152044 date "1993-08-01" @default.
- W1552152044 modified "2023-10-16" @default.
- W1552152044 title "Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves." @default.
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- W1552152044 doi "https://doi.org/10.1016/s0021-9258(17)46829-3" @default.
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