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Ricin and abrin are


Abrin is a plant toxin that is closely related to ricin in terms of its structure and chemical properties. DESCRIPTION: Abrin is an extremely toxic plant protein derived from the seeds of the plant Abrus precatorius. At least theoretically, the similarity of abrin to ricin gives it a similar potential as a bioterrorism agent.
Clinical manifestations are dependent on the route of exposure. Deliberate dissemination may occur as an aerosol, through addition to food or water, or by direct parenteral injection. It is obtained from the seeds of Abrus precatorius (commonly known as jequirity bean or rosary pea), a tropical vine cultivated as an ornamental plant in many locations.

In the body, these toxins inhibit protein synthesis leading to cell death. poison that occurs naturally in the castor bean plant which is used to make castor oil Neither abrin nor ricin are likely to Human toxicity of castor beans (ricin) and jequirity seeds (abrin) has been acknowledged throughout medical history, worldwide. Both plants are perennial in tropical and subtropical regions of the world. Abrin, like the similar plant toxin ricin, causes toxicity by inhibiting the formation (synthesis) of proteins in the cells of the exposed individual. Ricin and abrin are potent biological toxins that are derived from plant sources (castor beans and rosary peas, respectively). Abrin and ricin, two of the most potent toxins known, are produced in the seeds of the jequirity plant (Abrus precatorius) (Figure 1 a,b) and the castor plant (Ricinus communis) (Figure 1 c,d) respectively. The mechanism of ribosome inactivation by abrin is essentially identical to that of ricin. More is known about ricin toxicity; however, abrin toxicity is similar in its mechanism of action. Features Mechanisms of toxicity. Abrin and ricin can be prepared as a crude impure plant extract, purified crystals or powder forms, or solubilised in liquids. Abrin (and ricin… Like ricin, abrin is a type 2 ribosome-inactivating protein with A and B chains linked by a disulphide bond.

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