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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 195 (1986), S. 1-8 
    ISSN: 0014-5793
    Keywords: Immunotoxin ; Ribosome-inactivating ; Toxin ; protein
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 171 (1984), S. 277-279 
    ISSN: 0014-5793
    Keywords: Adenia volkensii ; Lectin ; Protein-synthesis inhibition ; Toxin ; Volkensin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 157 (1983), S. 150-154 
    ISSN: 0014-5793
    Keywords: Fusion ; Hybrid ; Microinjection ; Ribosome inactivating protein ; Sendai virus ; Toxin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1570-7458
    Keywords: Toxin ; insect pests ; RIPs ; insect nutrition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Résumé La ricine et la saporine des graines de plantes représentent deux classes différentes de protéines inactivant les ribosomes (RIPs), ou cytotoxines. La toxicité de ces substances pour plusieurs eucaryotes est bien connue, de même que le processus intracellulaire de leur activité inhibitrice des ribosomes. Cependant, on ne connaît pratiquement rien de leurs effets sur les insectes. Dans cet article, nour relatons des travaux systématiques qui montrent que les RIPs peuvent être extrêmement toxiques pour les insectes, bien que leurs effects varient suivant les ordres d'insectes. Particulièrement, deux espèces de coléoptères sont extrêmement sensibles aux effets des deux RIPs avec des DL50 inférieures à `0-2% du poids sec. Ces travaux indiquent aussi que la résistance des lépidoptères à ces effets toxiques peut être due en partie à la présence dans leur intestin de protéases susceptibles d'hydrolyser les RIPs, et de les éliminer ainsi avant leur absorption et avant qu'elles ne puissent exercer leurs effets dans les cellules des insectes.
    Notes: Abstract Ricin and saporin represent two different classes of ribosome inactivating proteins (RIPs), or cytotoxins, present in plant seeds. The toxicity of these substances to several eukaryotic organisms is widely known, as is their intracellular mode of inhibitory action on the ribosomes. However virtually nothing is known of the effects of these substances on insects. In this paper we report on systematic studies which indicate that RIPs can be extremely toxic to insects although the effects are variable with different insect orders. Specifically, two Coleopteran species were extremely susceptible to the effects of both RIP's with average LD50 values of less than 10-2% (dry weight). The studies also indicate that resistance to the toxic effects, exhibited by Lepidopteran insects, may be due in part to the protease complements of the insect guts which are capable of hydrolysing the RIPs, thus eliminating them before they are absorbed and can exert their effects within the insects cells.
    Type of Medium: Electronic Resource
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