Abstract
Ribosome-inactivating proteins (RIPs) display adenine polynucleotide glycosylase activity on different nucleic acid substrates, which at the ribosomal level is responsible for the arrest of protein synthesis. Some type 2 RIPs, namely ricin and related proteins, are extremely toxic to mammalian cells and animals whilst other type 2 RIPs (non-toxic type 2 RIPs) display three to four logs less toxicity. We studied whether a correlation exists between toxicity on cells and enzymatic activity on nucleic acids. All type 2 RIPs differ in their depurinating activity on the different substrates with differences of up to one to two logs. The toxicity of type 2 RIPs is independent of their enzymatic activity on nucleic acids or on ribosomes.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Abrin / toxicity
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Algal Proteins
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Animals
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Enzymes / metabolism*
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Glycoproteins / toxicity
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Microsomes, Liver / chemistry
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N-Glycosyl Hydrolases / metabolism
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Plant Lectins / metabolism
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Plant Lectins / toxicity
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Plant Preparations / toxicity
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Plant Proteins / metabolism
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Proteins / metabolism
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Rats
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Ribosomal Proteins / metabolism*
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Ribosome Inactivating Proteins
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Ribosome Inactivating Proteins, Type 2
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Ribosomes / metabolism
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Ricin / toxicity
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Substrate Specificity
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Toxins, Biological / toxicity
Substances
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Algal Proteins
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Enzymes
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Glycoproteins
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Plant Lectins
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Plant Preparations
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Plant Proteins
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Proteins
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Ribosomal Proteins
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Ribosome Inactivating Proteins, Type 2
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Ricinus communis agglutinin-1
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Sambucus nigra lectins
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Toxins, Biological
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ebulin r protein, Sambucus ebulus
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ribosome inactivating protein, Viscum
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cinnamomin, Phytophthora cinnamomi
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Abrin
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modeccin
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Ricin
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volkensin
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N-Glycosyl Hydrolases
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Ribosome Inactivating Proteins