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Studies on the proteins from the seeds of Croton tiglium and of Jatropha curcas. Toxic properties and inhibition of protein synthesis in vitro.
The crude protein from both seeds and peaks I and II from Croton and peak I from Jatropha were toxic to mice, to different extents, and inhibited protein synthesis by a reticulocyte lysate. Expand
Damage to nuclear DNA induced by Shiga toxin 1 and ricin in human endothelial cells 1
It is shown that RIPs can damage nuclear DNA in whole cells by means that are not secondary to ribosome inactivation or apoptosis, and such damage is consistent with the enzymatic activity of RIPs acting in vitro on RNA‐free chromatin and DNA. Expand
The RNA-N-glycosidase activity of Shiga-like toxin I: kinetic parameters of the native and activated toxin.
Shiga toxin and Shiga-like toxins are ribosome-inactivating proteins with RNA-N-glycosidase activity which remove a specific adenine from 28S RNA. The toxins are composed of an A subunitExpand
Purification and properties of different forms of modeccin, the toxin of Adenia digitata. Separation of subunits with inhibitory and lectin activity.
1. The subunits were isolated of modeccin (subsequently referred to as modeccin 4B), the toxin purified from the roots of Adenia digitata by affinity chromatography on Sepharose 4B [Gasperi-Campani,Expand
Inhibition of protein synthesis in vitro by proteins from the seeds of Momordica charantia (bitter pear melon).
The proteins seem to act catalytically, since they inactivate a molar excess of ribosomes in the lysate system, and are somewhat toxic to mice. Expand
High-pressure-liquid-chromatographic and fluorimetric methods for the determination of adenine released from ribosomes by ricin and gelonin.
The high fluorescence of adenine-containing compounds after reaction with chloroacetaldehyde was used to measure the adenine released from rat liver and Artemia salina ribosomes by the action ofExpand
A rapid and sensitive method to measure the enzymatic activity of ribosome-inactivating proteins.
The method, which measures directly the [3H]adenine released, is highly specific, extremely rapid and quantitative in a wide range of RIP concentrations. Expand
Inhibition by ricin of protein synthesis in vitro. Ribosomes as the target of the toxin.
It is suggested that ricin brings about an irreversible modification of ribosomes which impairs their ability to interact with EF 2, and since ricin inhibits at a molar concentration much lower than that of Ribosomes it probably acts catalytically. Expand
Inhibition by ricin of protein synthesis in vitro. Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes.
The binding of EF2 (elongation factor 2) and of ADP-ribosyl-EF 2 to rat liver ribosomes is inhibited by ricin. This result suggests that the native enzyme and its ADP-ribose derivative have the sameExpand