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Ribosome-inactivating proteins (RIPs) from plants inactivate eukaryotic ribosomes, as far as studied by rendering their 60 S subunit unable to bind elongation factor 2. These proteins seem widely distributed and possibly ubiquitous in plants. They are either type 1, those consisting of a single poly...

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Bibliographic Details
Published in:FEBS Letters 1986-01, Vol.195 (1), p.1-8
Main Authors: Stirpe, Fiorenzo, Barbieri, Luigi
Format: Article
Language:English
Subjects:
Antibodies - administration & dosage
Antibody Formation - drug effects
ID50, concentration causing 50% inhibition
Immunotoxin
Molecular Weight
PAP, pokeweed antiviral protein (prepared from seeds, PAP-S)
Plant Proteins - classification
Plant Proteins - pharmacology
protein
Protein Biosynthesis - drug effects
Ribosome-inactivating
Ribosomes - drug effects
RIP(s), ribosome-inactivating protein(s)
Terminology as Topic
Toxin
Toxins, Biological - pharmacology
Toxins, Biological - therapeutic use
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Summary:Ribosome-inactivating proteins (RIPs) from plants inactivate eukaryotic ribosomes, as far as studied by rendering their 60 S subunit unable to bind elongation factor 2. These proteins seem widely distributed and possibly ubiquitous in plants. They are either type 1, those consisting of a single polypeptide chain, or type 2 (ricin and related toxins), those consisting of two chains, one of which is a galactose-binding lectin. The literature on RIPs from 1982 has been reviewed with respect to (i) the chemical and biological properties of RIPs, (ii) their use for the preparation of immunotoxins and (iii) new perspectives.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)80118-1