Abstract
The bark of Sambucus nigra L. contains a non-toxic novel type 2 ribosome-inactivating protein that we named nigrin b. In vitro, nigrin b strongly inhibited mammalian protein synthesis but did not affect plant nor bacterial protein synthesis. The protein (M(r) 58,000) contains two subunits, A (M(r) 26,000) and B (M(r) 32,000); linked by disulphide bridge(s). Nigrin b was found to be an rRNA N-glycosidase of the rRNA of intact mammalian ribosomes and shares a very good N-terminal amino-acid sequence homology with the anti-HIV-1 proteins TAP 29 and trichosanthin.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Chromatography, High Pressure Liquid
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Hemagglutination Tests
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Molecular Sequence Data
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N-Glycosyl Hydrolases / chemistry
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N-Glycosyl Hydrolases / isolation & purification*
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N-Glycosyl Hydrolases / pharmacology
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Plant Proteins / isolation & purification*
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Plant Proteins / pharmacology
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RNA, Ribosomal / metabolism
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Rabbits
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Rats
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Ribosome Inactivating Proteins
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Ribosome Inactivating Proteins, Type 2
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Ribosomes / drug effects*
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Sequence Homology, Amino Acid
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Trees / chemistry*
Substances
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Plant Proteins
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RNA, Ribosomal
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Ribosome Inactivating Proteins, Type 2
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N-Glycosyl Hydrolases
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Ribosome Inactivating Proteins