Fact Sheet About Poisoning From Ricin Toxin Ricin Poisoning Facts Fact Sheet about Poisoning from Ricin Toxin Castor beans are the source of the poison called ricin, but they are also the source of castor oil and other products. You can hold the seeds in your hand and grow the plants in your garden to repel pests. Anne Helmenstine Ricin is a potent toxin extracted from castor beans. There is a lot of fear and misinformation associated with this poison. The purpose of this fact sheet is to help separate fact from fiction regarding ricin poisoning. What Is Ricin? Ricin is a protein that is naturally found in castor beans (Ricinus communis). It is so powerful a poison that the US Centers for Disease Control (CDC) estimate the lethal dose in humans is about the size of a grain of salt (500 micrograms injected or inhaled). How Is Ricin Used as a Poison? Ricin is poisonous if it is inhaled, eaten, or injected. It can be dissolved in water or weak acid and added to a drink. It is not absorbed through the skin, so simply touching ricin or getting ricin powder in your eyes will not cause poisoning.

What Are the Symptoms of Ricin Poisoning? Symptoms of ricin poisoning show up a few hours after exposure. The symptoms depend on the route of exposure. Inhalation Symptoms from ricin inhalation would include coughing, shortness of breath, and nausea. continue reading below our video 4 Tips for Improving Test Performance Fluid would begin to accumulate in the lungs. Fever and excessive sweating would be likely. Low blood pressure and respiratory failure could lead to death. Ingestion Eating or drinking ricin would produce cramping, vomiting, and bloody diarrhea leading to extreme dehydration. Bleeding from the stomach and intestines would occur. The victim may experience hallucinations, seizures, and bloody urine. Eventually (usually after several days) the liver, spleen, and kidneys could fail. Death would result from organ failure. Injection Injected ricin produces swelling and pain in the muscles and lymph nodes near the site of the injection. As the poison worked its way outward, internal bleeding would occur and death would result from multiple organ failure. How Is Ricin Poisoning Detected and Treated? Ricin poisoning is not easy to detect, but it is not necessarily fatal, even though it is unlikely medical staff would identify the underlying cause.

Treatment addresses the symptoms of ricin poisoning and includes helping the victim breathe and administering intravenous fluids to combat dehydration and low blood pressure. Death usually occurs 36-48 hours after exposure, but if a victim survives approximately 5 days, he has a good chance of recovering. Victims of ricin poisoning typically sustain permanent organ damage. How Does Ricin Work? Ricin inactivates the ribosomes in cells making them unable to produce proteins. Cells need these proteins to survive and reproduce, so when ribosomes are inactivated, cells die. What Should You Do If You Suspect Ricin Poisoning? If you believe you have been exposed to ricin you should move away from the location of the poison. Seek immediate medical attention, explaining to the medical professional that you believe you were exposed to ricin and the circumstances of the event. Remove your clothing. Cut off clothing rather than pulling it over your head, to minimize further exposure. Remove and discard contact lenses. Glasses may be thoroughly washed with soap and water and re-used. Wash your entire body with soap and water.

Cornell University Department of Animal Science Ricin Toxin from Castor Bean Plant, Ricinus communis Ricin is one of the most poisonous naturally occuring substances known. The seeds from the castor bean plant, Ricinus communis, are poisonous to people, animals and insects. One of the main toxic proteins is "ricin", named by Stillmark in 1888 when he tested the beans' extract on red blood cells and saw them agglutinate. Now we know that the agglutination was due to another toxin that was also present, called RCA (Ricinus communis agglutinin). Ricin is a potent cytotoxin but a weak hemagglutinin, whereas RCA is a weak cytotoxin and a powerful hemagglutinin. Poisoning by ingestion of the castor bean is due to ricin, not RCA, because RCA does not penetrate the intestinal wall, and does not affect red blood cells unless given intravenously. If RCA is injected into the blood, it will cause the red blood cells to agglutinate and burst by hemolysis. Perhaps just one milligram of ricin can kill an adult.

The symptoms of human poisoning begin within a few hours of ingestion. The symptoms are: a decrease in urine, and a decrease in blood pressure. If death has not occurred in 3-5 days, the victim usually recovers. It is advisable to keep children away from the castor bean plant or necklaces made with its seeds. In fact donít even have them in or around a house with small children. If they ingest the leaves or swallow the seeds, they may get poisoned. The highly toxic seeds beaded into necklaces, cause skin irritation at the contact point. If the seed is swallowed without chewing, and there is no damage to the seed coat, it will most likely pass harmlessly through the digestive tract. However, if it is chewed or broken and then swallowed, the ricin toxin will be absorbed by the intestines. It is said that just one seed can kill a child. Children are more sensitive than adults to fluid loss due to vomiting and diarrhea, and can quickly become severely dehydrated and die. Castor bean plants in a garden should not be allowed to flower and seed.

[Castor Bean Plant, Poisoning, and Oil] [Mechanism of Toxic Action] [Ricin Biosynthesis] [Ricin Enzymatic Action] [Ricin Structure] [Ricin Uptake] [Therapeutic Applications of Immunotoxins] [Toxigenic Ablation] [References] [Return to list of toxicants] Castor Bean Plant, Poisoning, and Oil The castor bean plant, Ricinus communis, is a "native of tropical Africa cultivated in several varieties for the oil found in its leaves and for its bold foliage."(Alber and Alber) The "stalked leaves consist of usually eight radiating, pointed leaflets with slightly serrated edges and prominent central veins. Many varieties are green, but some are reddish brown."(Cooper and Johnson) The flowers are green and inconspicuous, but pink or red in the pigmented varieties. Many stamens are near the base and branching pistils are near the top of the flower. The soft-spined fruits containing attractively mottled seeds are distinctive features of the plant.

It is grown as an ornamental in gardens, sometimes as a houseplant, and also grows as a weed. It is an annual in the south and a perennial in the tropics, and it may reach "15 feet tall outdoors". It is a woody herb belonging to the family of Euphorbiacea (Spurge). For further details on the plantís characteristics, see "Poisonous Plants Page, Ricinus Communis, Castor bean poisoning - Children It is advisable to keep children away from the castor bean plant or necklaces made with its seeds. In fact don't even have them in or around a house with small children. If they ingest the leaves or swallow the seeds, they may get poisoned. The highly toxic seeds beaded into necklaces, cause skin irritation at the contact point. If the seed is swallowed without chewing, and there is no damage to the seed coat, it will most likely pass harmlessly through the digestive tract. However, if it is chewed or broken and then swallowed, the ricin toxin will be absorbed by the intestines. It is said that just one seed can kill a child.

Children are more sensitive than adults to fluid loss due to vomiting and diarrhea, and can quickly become severely dehydrated and die. Castor bean plants in a garden should not be allowed to flower and seed. A good practice is to "nip it in the bud". Murder In 1978, ricin was used to assassinate Georgi Markov in 1978, a Bulgarian journalist who spoke out against the Bulgarian government. He was stabbed with the point of an umbrella while waiting at a bus stop near Waterloo Station in London. They found a perforated metallic pellet embedded in his leg that had presumably contained the ricin toxin. Animals Aphids, drawn to the right on a leaf of the castor bean plant, are susceptible to poisoning from ingesting the phloem. The sap-suckers died within 24 hours of feeding. The European corn borer and the Southern corn rootworm larvae were killed when exposed to feed painted with 2% ricin. Studies like these are undertaken to develop "natural" pesticides. Castor beans are used as an ingredient in some animal feeds after the oil has been extracted or inactivated by heating for 20 minutes at 140oC.

Attempts to use castor beans in feed for livestock involve different methods of inactivating ricin while maintaining nutritional value. Some studies have shown that even afte such heat treatment, toxicity remains. For example, it was lethal to mallard ducks given the feed. "The toxicity of the meal could be due to either a heat stable or growth inhibiting factor or due to minute residues of ricin"(Okoye et al.) A study with sheep showed that autoclaved castor-bean-meal can be incorporated to 10% of sheep rations without any ill effect. Poisoning of livestock usually occurs by accidental incorporation of castor beans in their feed. Horses are particularly vulnerable. For more detailed information about effects of Ricin on livestock, see... "Poisonous Plants Page, Ricinus Communis, Castor oil Castor beans are pressed to extract castor oil which is used for medicinal purposes. Ricin does not partition into the oil because it is water-soluble, therefore, castor oil does not contain ricin, provided that no cross-contamination occurred during its production.

More information describing this plant is available under the listing for Ricinus communis , Castor Bean, in the Canadian Poisonous Plants Information System, courtesy of Derek B. Munro. Mechanism of Toxic Action Many cytotoxic proteins from a variety of plants have been identified, and they are related to ricin both in structure and function. They inhibit protein sythesis by specifically and irreversibly inactivating eukaryotic ribosomes. These "ribosome-inactivating proteins" (RIPs) are typically N-glycosylated, 30 kDa monomers (Type 1 RIPs). However, in order to bind to the cell surface galactosides and enter the cytosol to reach ribosomes, they require a second monomer, a galactose-binding, 30 kDa lectin. The monomers are joined by a disulfide bridge to form the toxic heterodimers (Type 2 RIPs). Some plants, such as wheat andbarley, have only Type 1 RIPs, and are not poisonous, while others, such as the castor bean plant seed, contain the Type 2 RIPs that are among the most potent cytotoxins in nature.

5% of the Ricinus seed consists of ricin and RCA (Ricinus communis agglutinin). Ricin is a heterodimeric type 2 RIP. This ribosome-inactivating enzyme (32 kDa), also known as the A chain, is linked by a disulfide bond to the galactose/N-acetylgalactosamine-binding lectin (34 kDa), also called the B chain. Ricin Biosynthesis Ricin and RCA are synthesized in the endosperm cells of maturing seeds, and are stored in an organelle called the "protein body", a vacuolar compartment. When the mature seed germinates, the toxins are destroyed by hydrolysis within a few days. Ricin begins sythesis as a prepropolypeptide that contains both A and B chains. The signal sequence of the Nh3-terminus targets the nascent chain to the endoplasmic reticulum (ER) and is then cleaved off. As the proricin polypeptide elongates it is N-glycosylated within the lumen of the ER.

Protein disulfide isomerases catalyze disulfide bond formation as the proricin molecule folds itself. Proricin undergoes further oligosaccharide modifications within the Golgi complex and then is transported within vesicles to the protein bodies. Ricin is not catalytically active until it is proteolytically cleaved by an endopeptidase within the protein bodies. This splits the polypeptide into the A chain and the B chain still linked by a single disulfide bond. Since ricin is inactive until then, the plant avoids poisoning its own ribosomes in case some proricin accidentally passes into the cytosol during synthesis and transport. Ricin Enzymatic Action The ricin A portion of the heterodimer is the enzyme that binds and depurinates a specific adenine of the 28S rRNA. The adenine ring of the ribosome becomes sandwiched between two tyrosine rings in the catalytic cleft of the enzyme and is hydrolyzed by the enzymeís N-glycosidase action. The target adenine is a specific RNA sequence that contains the unusual tetranucleotide loop, GAGA.

Ricin is more active against animal than plant ribosomes, and intact bacterial ribosomes are generally not susceptible. Ricin Structure This figure from Lord et al, depicts a 3-dimensional ribbon drawing of ricin, modeled from X-ray crystallography data. The upper right half, the dotted ribbon, is the A chain, and the lower left half, the solid ribbon, is the B chain. The A chain (or RTA)is a 267-amino acid globular protein. It has 8 alpha helices and 8 beta sheets. The substrate binding site is the cleft marked by the substrate adenine ring. The B chain (or RTB) is a 262-amino acid protein that is shaped like a barbell. It has a binding site for galactose at each end, (depicted by lactose rings). These two sites allow hydrogen bonding to specific membrane sugars (galactose and N-acetyl galactosamine). A disulfide bridge (-S-S-) joins RTA with RTB (far-right, center). The spheres are trapped water molecules.

Ricin Uptake The RTB portion of ricin binds to both glycoproteins and glycolipids at cell surfaces that terminate with galactose. It has two binding sites for galactose, and 106 to 108 ricin molecules may bind per cell. However, just a single ricin molecule that enters the cytosol can inactivate over 1,500 ribosomes per minute and kill the cell. As shown in the diagram, the pathway for internalization of ricin involves: endocytosis by coated pits and vesicles or, endocytosos by smooth pits and vesicles. The vesicles fuse with an endosome. Many ricin molecules are returned to the cell surface by exocytosis, or the vesicles may fuse to lysosomes where the ricin would be destroyed. If the ricin-containing vesicles fuse to the Trans Golgi Network, (TGN), thereís still a chance they may return to the cell surface. Toxic action will occur when RTA, aided by RTB, penetrates the TGN membrane and is liberated into the cytosol.

Once inside the cytosol, the RTA catalyzes the depurination of the ribosomes, halting protein synthesis. Therapeutic Applications of Immunotoxins Ricin can be targeted to specific cells, such as cancer cells, by conjugating the RTA subunit to antibodies or growth factors that preferentially bind the unwanted cells. These immunotoxins have worked very well for in vitro applications, e.g. bone marrow transplants. Although they have not worked very well in many in vivo situations, progress in this area of research shows promise for the future. IN VITRO APPLICATIONS In bone marrow transplant procedures, RTA-immunotoxins have been used successfully to destroy T lymphocytes in bone marrow taken from histocompatible donors. This reduces rejection of the donor bone marrow, a problem called "graft-vs-host disease" (GVHD). In steroid-resistant, acute GVDH situations, RTA-immunotoxins helped alleviate the condition. Also, in autologous bone marrow transplantation, a sample of the patients own bone marrow is treated with anti-T cell immunotoxins to destroy malignant T-cells in T cell leukemias and lymphomas.

IN VIVO APPLICATIONS "For the in vivo treatment of solid tumors, considerable problems can arise due to poor access of the immunotoxin (IT) to the tumor mass; lack of IT specificity, tumor cell heterogeneity, antigen shedding, breakdown or rapid clearance of the IT, and dose-limiting side effects". (Lord et al.). One common problem encountered in patients treated with ricin-immunotoxins is the "vascular leak syndrome", in which fluids leak from blood vessels leading to hypoalbuminemia, weight gain and pulmonary edema. "Research efforts to expand and develop immunotoxins and therapies for clinical use in cancer and AIDS are continuing with strategies utilizing recombinant DNA technology (Lord et al.). Toxigenic Ablation Toxigenes "Toxigenes are DNA fusions in which DNA encoding a potent toxin, e.g. RTA, is placed under the transcriptional control of a tissue- or developmental stage-specific promoter and/or enhancer. When expressed intracellularly, the toxigene product causes cell death.

The introduction and expression of a toxigene in transgenic animals or plants may lead to cell type-specific ablation, which can be used to study developmental cell lineages or to generate animal models of degenerative diseases." (Lord et al.) Suicide Transport Diagram shows injection of ricin into vagal nerve and subsequent destruction of neurons (dashed neurons destroyed, solid neurons unaffected). Neuroscientists can selectively destroy neurons by injecting ricin into nerves. Retrograde axonal transport mechanisms bring the toxin to the neuronal cell bodies where the ribosomes are localized. Ultrastructural analysis reveals that ricin first causes the dispersion of polyribosomes, and then the rough endoplasmic reticulum disorganizes into smooth vesicles. The cell bodies (perikaryon) swell, the nuclei degenerate and the entire neuron disintegrates. Since ricin is a N-acetyl galactosamine-binding lectin, it can be used with different lectins that have different specificities tomap neuronal patterns of glycosylation. When suicide transport is observed after injection of the toxin, it confirms the presence of N-acetyl galactosamine residues on the neuronal cell surface.

Strategies in suicide transport work very well in studies of adult peripheral sensory and motor neurons because they are sensitive to ricin. Neurons in the central nervous system of adults are resistant to ablation by ricin, whereas young developing brains are sensitive, suggesting that brain development involves changes in glycosylation of CNS neurons. The galactose terminal residues may be either clipped or masked by addition of sialic acids residues. In suicide transport experiments, often some ricin leaks out of the nerve, causing systemic poisoning of the animal. This problem can be avoided by simultaneously administering a ricin antiserum. The value of using suicide transport strategies is summarized (from Wiley and Oeltmann): anatomical mapping of neurons modeling of motor neuron degenerative diseases studying consequences of peripheral nerve damage and repair mechanisms mapping cellular neurotransmitter receptors Castor Bean (Ricinus communis) Toxicity - Pet Tools Inc. Castor Bean (Ricinus communis) Toxicity By pettoolsvet on August 4, 2013 in Plants , Toxic & Not Castor bean or Ricinus communis is a member of the Euphorbia family, and is the only species in its genus.

It originated in the Middle East and India, but is widely grown as an ornamental plant and for oil production. Castor oil, which has had both industrial and medicinal uses is extracted from the seed. The seed also has the highest concentration of ricin, a potent toxin. Extracts have been used for insecticidal purposes. The seeds are sometimes used in necklaces and bracelets, offering an creating a potential for both children and pets to be exposed to the toxin. As the plant is easily available, ricin is a potential terrorist weapon. The Bulgarian dissident, Gorgi Markov, was killed in 1978 by a ricin pellet injected on a London street. Heating according to specific protocols inactivates ricin and permits castor oil to be used industrially. There also has been some investigation to see if a modified ricin protein can be used in cancer treatment. The waste material left after the castor oil is extracted is often used as a fertilizer or as a feed. In the case of feed, it is critical that this material be heat treated to inactivate the toxin and even then some toxicity may persist. Such feed has been lethal to duck; ruminants seem the most tolerant.

Beans have been accidentally ingested in people, dogs and horses. Ingestion of castor bean waste material where the toxin was not inactivated by heat has been fatal to dogs. Toxic mechanism Ricin is a protein that binds to a ribosome subunit, killing cells by inhibiting protein synthesis. It also appears to affect the calcium balance in the heart which can lead to cardiac hemorrhage and cell death.. It is thought to be one of the most toxic plant substances known to man, causing multi-organ failure. Developing brains are particularly sensitive. Inhalation or injection is much more toxic than ingestion. The seeds have a hard coat and seeds with unbroken coats may pass through the digestive tract with little effect. Chewing or grinding makes the toxin available. A large protein, it is poorly absorbed by the GI tract but its potency requires little absorption for effect. The oral lethal dose in humans for ricin is estimated at 5 mg/kg (~5 beans in a child; ~20 in an adult) and 20 mg/kg in dogs and cats. Symptoms Initial symptoms often depend on route of exposure, with clinical signs often not appearing for 8 to 24 hours.

In inhalation exposure anorexia and respiratory distress are commonly seen first. In oral exposure anorexia, vomiting and diarrhea, with or without blood, abdominal pain and depression are seen initially. Respiratory distress and pulmonary edema are common, cardiac abnormalities, cyanosis, hypotension, adrenal insufficiency affecting electrolytes, convulsions, coma, renal failure, liver failure, shock, death can occur. There may then be an apparent recovery, with late phase toxicity may be seen 2 to 5 days later with damage to blood cells, the central nervous system, liver, kidneys, spleen and adrenal system, with organ specific symptoms related to the degree to which an organ system has been affected by hemorrhage and tissue death .. Recovery many take time. In an analysis of 98 cases of dogs reported to a poison control center in 11 years, the fatality rate by death was 5% and by death and euthanasia was 9% Survivors of late phase toxicity may have permanent organ damage; fortunately many organs have considerable reserves. Diagnosis Diagnosis is usually by symptoms and history showing possible exposure. Some state and provincial veterinary toxicology labs have assays.

Differential diagnoses include zinc phosphide, vomitoxin, arsenic, lead, mercury, thallium, garbage poisoning and bacterial and viral infection with GI manifestations. Treatment In cases of known early ingestions before symptoms are seen, induction of vomiting or other decontamination by a veterinarian may be best; activated charcoal can also be useful if vomiting is absent. Magnesium sulfate or sorbitol may be used as a cathartic, if no diarrhea is present. If decontamination is effective, the animal can be observed at home. In symptomatic cases there is no antidote, aggressive supportive care is important with monitoring of electrolytes, aggressive fluid therapy to treat hypotension, medication to treat seizures, low blood pressure and acidosis. Severe cases may require ventilation support. Diuresis may help mitigate kidney damage due to hemoglobin released by bleeding. More information What Is Ricin | Bioterrorism Ricin Credit: Xico Putini | Shutterstock.com An envelope sent to U.S. Sen. Roger Wicker of Mississippi and intercepted by a government mail facility on Tuesday, April 16, has tested positive for ricin, a powdery, white poison.

And today, preliminary reports indicate a letter sent to President Barack Obama also tested positive for ricin. What is this deadly substance? Ricin is derived from a common plant, the castor bean (Ricinus communis), native to the Mediterranean and Middle East and cultivated elsewhere as an ornamental plant. It's also the source of castor oil, which has many uses in medicine, food and industry. [ The 10 Most Poisonous Common Plants ] But the plant is also linked to murderous, diabolical plots worthy of a spy thriller: Ricin is a highly potent toxin that can kill a person in amounts as small as a few grains of sand. According to the Centers for Disease Control and Prevention (CDC), just chewing and swallowing castor beans can cause serious injury. Ricin is easily derived from the waste made by processing castor beans. In 1969 — when Bulgaria was still part of the Soviet Bloc — a political dissident named Georgi Markov defected from Bulgaria, eventually settling in London, where he campaigned vigorously against Soviet oppression. While waiting for a bus on a London street in 1978, Markov was poked in the leg by the tip of someone's umbrella.

The umbrella, it turns out, stung Markov with a tiny amount of ricin. He died shortly thereafter, and his murderer (suspected of being a Soviet agent) was never found. Ricin kills by inhibiting protein synthesis in cells, according to the CDC. Symptoms of ricin poisoning, which can take several hours to show up, vary depending on whether the toxin was inhaled, ingested or — as in the case of Markov — injected. Symptoms may include fever, difficulty breathing, fluid in the lungs, vomiting, diarrhea , dehydration and blood in the urine. Death can result within 72 hours; even survivors may have long-term organ failure and other health problems. There is no known antidote for ricin poisoning. Despite its deadly nature — or because of it — ricin has been investigated for medicinal uses, including cancer treatment, according to the National Terror Alert Response Network. Ricin may have the potential to target and kill cancer cells. As a bioterrorism weapon, ricin is of limited concern to security experts, since it's better suited to small-scale attacks on individuals than large groups, the Associated Press reports.

Compared with other terrorist weapons, "it is one of the least significant; it is a poison," University of Maryland bioterrorism expert Milt Leitenberg told the AP. Nonetheless, the New York Times reported in 2011 that an al-Qaida group in Yemen was trying to acquire large amounts of castor beans to produce ricin bombs. In 2004, ricin was found in a letter in a U.S. Capitol mailroom that served then-Majority Leader Bill Frist, CNN.com reports. Sixteen mailroom employees went through decontamination procedures; none reported any ill effects. Other bioterrorism agents such as anthrax are of greater concern to security experts. In 2001, letters containing anthrax were sent to two members of Congress and several news organizations. In those attacks, five people died and 17 were sickened. Follow Marc Lallanilla on Twitter and Google+ . Follow us @livescience , Facebook & Google+ . Original article on LiveScience.com .

Editor's Recommendations Science Everything You Need To Know About Ricin, The Poison Mailed To President Obama Ricin is one of the most poisonous substances on Earth, it's scarily easy to make, and somebody is mailing it to the President and at least one U.S. senator. What it is, how it works, and more, inside. By Dan Nosowitz posted Apr 17th, 2013 at 2:30pm via Breaking Bad Wiki Ricin (on Breaking Bad) Yesterday, an envelope addressed to Senator Roger Wicker, Republican of Mississippi, was found to contain a white granular substance that was identified as ricin. Today, a similar letter addressed to President Obama was found. These envelopes were intercepted off-site--they never got anywhere near their targets--but as a precaution, Capitol Police have shut down mail service until they can figure out what's going on. In the meantime, let's talk about ricin! How poisonous is it? Oh, man. Very. It's dangerous in just about any way it gets into your system, though ingesting (eating) it is about the least dangerous way.

Injecting or inhaling requires about a thousand times less ricin to kill a human than ingesting, and that's a very small amount indeed. An average adult needs only 1.78mg of ricin injected or inhaled to die; that's about the size of a few grains of table salt--which ricin resembles visually. Wikimedia Commons The seeds of the castor plant, from which castor oil (and ricin) are extracted. How does it work? Ricin, a toxic protein, infects cells, blocking their ability to synthesize their own protein. Without cells making protein, key functions in the body shut down; even in survivors, permanent organ damage is often the result of ricin poisoning. It's a highly unpleasant way to be poisoned: within six hours, according to the Center for Disease Control, victims who have ingested ricin will feel gastrointestinal effects like severe vomiting and diarrhea, which can lead to serious dehydration. Then the ricin infects the cells of the vital gastrointestinal organs as they pass through the body, leading to the failure of the kidneys, liver, and pancreas.

Inhalation of ricin has a different effect, since the ricin proteins aren't interacting with the same parts of the body. Instead of gastrointestinal problems, you'll develop a vicious, bloody cough, your lungs will fill with fluid, and eventually you'll lose your ability to breathe, causing death. Injection, too, is different, depending on where you've been injected, but will generally result in vomiting and flu-like symptoms, swelling around the place of injection, and eventually organ failure as your circulatory system passes the protein around the body. Death from inhalation or injection usually occurs about three to five miserable, agonizing days after contact. Interestingly, there aren't any immediate symptoms, and indeed there can be a significant delay before symptoms show themselves, up to a day or two. Exposure on the skin is generally not fatal, though it may cause a reaction that can range from irritation to blistering. That sounds...horrible. Is there an antidote, at least? Haha. No. The US and UK governments have been working on an antidote for decades-- here's a nice article describing the progression of one such antidote--but there isn't one available to the public.

The CDC's website states bluntly, "There is no antidote for ricin toxicity." There are some steps you can take if you get to a hospital immediately; for ingestion, a stomach pump can sometimes prevent the ricin from reaching the rest of the gastrointestinal system at its full force. But...that's about it, really. Wikimedia Commons Castor Leaf How does it stack up against other poisons? Well, that depends on what your aim is. Ricin is much easier to produce than other popular biological weapons like botulinum, sarin, and anthrax, but it is not as potent as any of those, which limits its effectiveness as a weapon. It also is not very long-lived; the protein can age and become inactive fairly quickly compared to, say, anthrax, which can remain dangerous for decades. There were experiments back around World War I attempting to make wide-scale ricin weapons, packaging it into bombs and coating bullets in it, but these proved not particularly effective and also violate the Hague Convention's agreements on war crimes, so the US discarded ricin.

It's much more effective, weapon-wise, as a close-contact, small-target weapon--by injecting, as with Georgi Markov, or by putting small particles into an aerosol spray and blasting a target. It's also not contagious, which limits its effectiveness as a tool of biological warfare. But it's considered highly dangerous partly because it's still outrageously toxic and partly because it takes no great skill to produce. So it's not hard to make? Well...no. Like, not at all. It's made from the byproduct of the castor oil manufacturing process. You take the "mash" of the castor oil seeds, which contain around 5-10 percent ricin, and perform a process called chromatography. Chromatography is a blanket term for a set of techniques used to separate mixtures, usually by dissolving in liquid or gas. The US government has done its best to eradicate recipes for ricin from the internet, sort of; a patent was filed back in 1962 for ricin extraction, and the Patent Office took it off the publicly available server in 2004 for safety reasons.

That said, the recipe is super easy to find; here at the PopSci offices, I'm blocked from listening to Rdio on my work computer, but I found a recipe to make an outrageously deadly poison in about a minute. The techniques involved are undergraduate-level chemistry, creating a slurry with the castor bean mash and filtering with water and then a few easily-found substances like hydrochloric acid. It comes from castor beans? Ricin is a highly toxic protein that's extracted from the seed of the castor plant, often called a "castor bean" or "castor oil bean," despite not technically being a bean. The castor plant is extremely common; it's used as an ornamental plant throughout the western world, prized for its ability to grow basically anywhere as well as its pretty, spiky leaves and weird spiny fruits. It's also an important crop; the seeds are full of oil, and castor oil is used for lots of legitimate purposes. It's a common laxative, for one thing, and since it's more resistant to high temperatures than other kinds of vegetable oils, it's a nice alternative to petroleum oil in engines. Wait, but you can eat it? So how is this a poison?

Ah, yes. Castor oil is perfectly safe, according to the FDA and your grandma, but ricin is not castor oil. Castor seeds are still poisonous; this study says that a lethal dose of castor seeds for adults is about four to eight seeds. But the oil itself does not contain ricin; the ricin protein is left behind in the "castor bean mash" after the oil is extracted from the seed. Poisoning from eating the seed itself is rare. Have there been cases of ricin poisoning in the past? You mean, beyond the several times it's been featured as a major plot point in Breaking Bad? Sure! The most famous is probably the assassination of Georgi Markov in 1978. Markov was a Bulgarian novelist, playwright, journalist, and dissident, and was murdered by the Bulgarian secret service, with assistance from the KGB, by ricin injection. He was crossing a bridge when he was jabbed in the leg with an umbrella, which delivered a ricin pellet into his bloodstream. He died three days later of ricin poisoning.

There are plenty of incidents of people arrested for attempting (or, more often, succeeding) to make ricin; it's a pretty easy poison to make. In fact, there was even another ricin-in-the-envelope attempt made back in 2003--a person identifying as "Fallen Angel" sent letters filled with ricin to the White House, apparently as a result of some new trucking regulations (seriously). "Fallen Angel" was never found, but the letters were intercepted and did not cause any injury. Wikimedia Commons Ricin...How to extract ricin from castor beans. Ricin...How to extract ricin from castor beans. How to extract ricin from castor beans. WARNING Even the fumes given off during production are extremely toxic! You can kill yourself very easily making this! FULL HAZARDOUS MATERIAL PROTOCOLS MUST BE USED AT ALL TIMES! Copyright: Attribution Non-Commercial (BY-NC) 3 Ricin is just about the easiest, and at the same time, most toxic poisonthat a criminal can make. Less than a milligram (1/1,000 of a gram) injectedor inhaled will kill a person several times over.

For individual killings, it hasthe advantage of being undetectable in toxicology scans since the poison is acatalyst the starts a chain reaction in the body, and is destroyed before thesymptoms begin to show. With properly sized and dispersed dry particles, ricin is at least 10xmore toxic than the most potent nerve gas. A 1% water solution atomizedwith a small explosive burster has the same effectiveness as sarin nerve gas.The only disadvantage ricin has is the time it takes for the victims to die isabout 1 – 2 weeks. So you won’t have the quick tactical effect of nerve gas.But this can also be good in that, using a covert dissemination, the criminalhas time to escape before the attack is detected. The information presented below is from a US Patent #3,060,165 Tips Here’s a few things you need to know to make your production gomuch easier.The seeds are readily available through wholesale seed suppliers forabout $20 for a pound of seeds. Castor bean seeds are very tough to crack orpeel. Soak them for an hour in a solution of 2 tablespoons lye in 1 cup water.Then use pliers to crack the shell.

The shell will peel of the bean easily then. 1. Use a 1/2 cup of acetone to every ounce of bean pulp. Blend well.Let sit for several days with occasional shaking. Pour off the acetone andadd an additional 1/2 cup of acetone and repeat. This will remove almost allthe castor oil from the seeds. 2 . The patent doesn’t mention it, but you can use magnesium sulfate(Epsom salt) instead of sodium sulfate. Epsom salt is easily available in anydrug store for just about a dollar a pound. More From This User Ricin Ricin Introduction: Ricin is a protein composed of an A and B chain, with the single chains being found in barley and most wheat plants. What is commonly assumed when referencing “ricin” is the combination of A and B chains; this occurs naturally only in Castor beans. Ricin, in this form, is highly toxic and has been used extensively as a biological weapon. Ricin’s structure has a twofold impact, the B chain gains entrance into the cell allowing the A chain to mutate the rRNA by inactivating ribosomes (1).

Extensive research has been launched to gain a better understanding of ricin’s structure and pathways towards toxicity, this is in the hope that better antibodies can be produced, reducing the toxicity of ricin in humans (2). Ricin poses such a great threat, because of the miniscule dose required to be toxic. Ricin is so toxic because a one molecule of ricin in a cell’s cytosol can depurinate over 1500 ribosomes per minute, thusly resulting in the stop of protein synthesis. (1) The consequence of stopped protein synthesis is cell death, which can lead to abdominal pain and dehydration due to vomiting and diarrhea. Background The castor bean plant is an ornamental plant found in warm climates around the world. Ricin is found naturally in the castor bean, as they are a defense for the castor bean plant. Ricin is inadvertently produced during the extraction of castor oil from castor beans. The extraction process of castor oil begins with the washing and dehydration of the beans to 5% of their original moisture content. The beans are then crushed to weaken and rupture cell walls to aid in the release of the castor fat for extraction.

The crushed beans are then loaded into a mechanical press and the oil is extracted. The mechanical process results in about 45% recovery of oil. The other extraction method is solvent extraction, in which non-polar solvent and crushed castor beans are placed in a commercial extractor. The solvent extraction method heats the crushed seeds, thereby denaturing all of the ricin present (3). Castor oil has many uses, including medicinal use as a laxative and industrial uses as lubricants and as an ingredient in plastics, waxes, soaps, dyes, and paints. The castor bean mash, once denatured, can be used as animal feed (1). Ricin is toxic to humans and animals in extremely low doses. Improperly processed castor bean mash can result in the death of livestock. Ingestion of one castor bean can kill a child and several castor beans can kill an adult. The mechanical extraction does not involve heating the seed mash, therefore leaving the ricin non-denatured by the process of mechanical extraction. From the seed mash, ricin can be extracted and purified via chromatography.

The ricin is extracted from the seed mash with dilute acid, precipitated out of solution with ammonium sulfate, and then purified via column chromatography. Molecular Structure as it pertains to Toxicity Pathways Figure 1: Ricin. The A chain is the top right protein and the B chain is the bottom left protein. Note that the pairs of spheres in B chain represent two lactose moieties bound to B chain (4)(5). As previously stated, an A and B chain comprise ricin. The A chain is an N-glycoside hydrolase with three domains that form an active site cleft (as seen around residue 50 in Figure 1). Glycoside hydroloases, a process of breaking large sugar molecules into smaller ones and then releasing them, catalyze the hydrolysis of glycosidic linkage. In this case it cleaves a specific adenine residue from 28S rRNA. The A chain bonds in the cleft then breaks the single adenine disulfide bond to a galactose.

The N-glycoside hydrolase is composed of 267 amino acids, arrange primarily into α-helices and β-sheets (6). The B chain is a lectin composed of 262 amino acids, with lobes that contain three sub-domains that act as a sugar-binding pocket. The structure of the B chain allows ricin to bind to the terminal galactose on the cell. The B chain is lacking both α-helices and β-sheets; its structure, instead, forms a clover-shape. The B chain enters the cell by binding to the terminal galactose on the cell’s surface, the reducing atmosphere then cleaves the disulfide bond linking chains A and B. The A chain of ricin cleaves adenine from an adenosine nucleotide inside 28s rRNA. When A chain cleaves off the adenine, the ribosome is rendered inactive, thus having undergone depurination. The ribosome cannot bind to elongation factors when inactive (1). This covalent modification of ribosomal RNA is why ricin is toxic. Figure 2: The Toxicity Pathway for Ricin in mammalian cells (7).

As seen in Figure 2, ricin enters the cell via clathrin mediated endocytosis (7). Endocytosis is how cells internalize molecules and clathrin mediated endocytosis is the inward budding of plasma membranes containing receptor sites specific for the molecule to be internalized. Clathrin, a protein found in the receptor sites, does not have specificity towards ricin or other toxins, but it can mediate the entrance of such toxins into the cell. Once through the plasma membrane, the ricin travels to endosomes. From the endosomes, most of the ricin will be either recycled back to the surface or degraded in lysosomes. A small portion of the ricin will be transported to the trans golgi network (TGN) (8). The TGN is a complex network of membranes and vesicles that sorts and ships proteins to where they need to go based upon the molecular marker that they carry. From the TGN, ricin travels via the Golgi cisternae to the endoplasmic reticulum (ER). When ricin finally gets to the ER, the A chain crosses the membrane and depurinates ribosomes (9).

Ricin and other toxins that follow this toxicity pathway are extremely potent because most of the toxin gets degraded or recycled to the surface, leaving only a small fraction to terminate the cell (10)(7). Conclusion Ricin is toxic in very small doses and is relatively easy to manufacture, as the sale and cultivation of castor beans is not prohibited. Ricin is an extremely potent toxin, utilizing both its A and B chains to infiltrate and eviscerate the cell by depurinating ribosomes, preventing elongation. References Audi, J., Belson, M., Patel, M., Schier, J. Osterloh, J., Ricin Poisoning: A Comprehensive Review J. Am. Med. Assoc. 2005, 294 (18), 2342 – 2351. Endo, Y., Tsurugi, K., RNA N-Glycosidase Activity of A-chain, J. Biol. Chem.1987, 17(262), 8128 – 8130. Montfort, W., et al. The Three-dimensional Structure of Ricin at 2.8 Å, J. Biol.

Chem.1987, 262(11), 5398 – 5403. Ho, M.C. , Sturm, M.B. , Almo, S.C. , Schramm, V.L. Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins, Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 20276 – 20281. Dai, J., Zhao, L., Yang, H., Guo, H., Fan, K., Wang, Huaizu, Qian, W., Zhang, D., Li, B., Wang, Hao, Guo, Y. Identification of a Novel Functional Domain of Ricin Responsible for its Potent Toxicity, J. Biol. Chem. 2011, 289, 12166 – 12171. 6. Olsnes, S., The History of Ricin, Abrin, and related toxins, Toxicon 2004, 4(44), 361 – 370.

Lord, J.M., Roberts, L.M., Robertus, J.D., Ricin: structure, mode of action, and some current applications, FASEB J. 1994, 2(8), 201-208. Chen, X.Y. , Link, T.M. , Schramm, V.L. Ricin A-Chain: Kinetics, Mechanism, and RNA Stem-Loop Inhibitors, Biochemistry 1998, 37, 11605 – 11613. Lord, J.M., Roberts, L.M., Retrograde transport: Going against the flow, Curr. Biol.,1998, 8(2), R56 – R58. Ricin Toxin from Castor Bean Plant, Ricinus communis, 2009. Plants Poisonous to Livestock on Cornell University: Dept. of Animal Science. (Accessed on November 23, 2011) Patent US3060165 - Preparation of toxic ricin - Google Patents Preparation of toxic ricin Description (OCR text may contain errors) Oct.

23, 1962 H. L. CRAIG ETAL 3,060,165 PREPARATION OF TOXIC RICIN Filed July 3, 1952 LSlurry with waterI pH of 3.8 sou using 5% u so, LPrecipitate with N 80 pH of 7 using l2% Na,CO, l Wash filter cake with |6.7% M0 80 I Single extraction Wash solution Extract with wateri pH of 3.8#O.l using H 80 iii Precipitate with Na IpH of 7 using i2% Na ()0 [E'E l Wash filter cake with l6.7% No.80 I Wash solution Grind cake to 40 mesh Slurry with CCI. | Settle and skim oft Ricin i Settled M0 reuse I N VEN TORS Harry L. Craig 0. h. A/derks Alsop/l H. 00min Sally h. Die/re 0h affe L. Karel BY 4 14 W ATTORNEY Dry and grind States.

ate This invention relates to the method of preparing toxic llClIl. Ricin is a protoplasmic poison prepared from castor beans after the extraction of castor oil therefrom. It is most effective as a poison when injected intravenously or inhaled, the latter requiring extreme comminution and small particle size to be effective. It is believed that the toxic action is catalytic rather than stoichiometric which probably accounts for the high toxicity of the agent. Because of its relative instability, ricin must be handled with extreme care. In neutral aqueous solution it is stable only up to 60-75 C., and in solid form up to 100110 0, although for short exposures, temperatures up to 130 may be tolerated. It is sensitive to acids, alkalis and halogen and may also be inactivated by mechanical working such as grinding or pulverizing. These factors are of great importance in developing a satisfactory method for preparing the material. Although ricin has been prepared in crystalline condition in the laboratory in small quantities, it becomes necessary, for purposes of toxicological warfare, to prepare relatively large quantities in a high state of purity.

This necessitates that as much as possible of the non-toxic material present be removed in the process. In preparing the protein material, the castor beans are first ground and pressed to remove most of the oil. The pressed cake still retains about 15% oil and this may be removed by means of solvents which will extract an additional 150 pounds of oil per ton of beans and reduce the oil retained in the cake to a little over 1%. In the event that the expressing step is supplemented by solvent extraction, it is important to prevent detoxification of the protein during the solvent removal step. If residual solvent is removed from the ground beans by blowing with steam, considerable detoxification results. Blowing with nitrogen efiectively prevents detoxification but is expensive when carried out on a large scale. After the oil has been removed, the pressed cake or pomace is extracted by agitating with water at a pH of 3.8101 at 25 C. which removes substantially all of the toxic protein.

The extraction process is operative within a pH range of about 3 to 4.5 although the preferred range is about 3.5 to 4., The optimum operating point is a pH of 3.8-1.1, as indicated above. A careful pH control is essential in order that as much non-toxic protein as possible may be eliminated and also that the filtration rate may be held at a satisfactory value. Either HCl or H 80 may be used to get the desired pH for the extraction water, but H 50 is preferred due to its lower corrosion rate and ease of handling in concentrated form. The acid should be used in reasonably dilute form to prevent undue local concentrations during its addition. A 5% concentration is satisfactory. Following the extraction, the slurry is filtered using either a conventional recessed plate filter or a continuous string discharge vacuum filter. With the latter about 7% of filter aid, based on meal weight, was found necessary for satisfactory filtration. The filtrate from the water extraction step, which contains the ricin, was treated with a 16.7% solution of Na SO to precipitate the protein.

This solution is com- "ice posed of 20 pounds of salt in 100 pounds of water and the amount used was such that the salt content equalled 20% of the filtrate weight. This amount and concentration of salt solution was about optimum considering the factors of cost and toxin recovery. Somewhat higher concentrations and larger amounts of solution can be used, however. The precipitation process is not limited to the use of Na SO since a saturated solution of NaCl can be used successfully, but Na SO solution gives better nitrogen fractionation, more rapid precipitation, and can be operated under wider pH limits. It is desirable to raise the pH to about 7-8 before precipitation as this gives better ecovery and greater non-toxic nitrogen removal. The pH was raised to this value by using NaOH or Na CO the latter being preferred. The base used was quite dilute in order to prevent detoxification due to high local concentrations in the solution. A 5% solution of NaOH was used, whereas with Na CO a 12% solution was preferred. In general, this higher pH during precipitation gave a greater non-toxic nitrogen fractionation and at the same time maintained the toxin loss at less than 2%.

After precipitation, the slurry was filtered using from 1 to 4% filter aid, based on slurry weight, for satisfactory filtration; the amount of filter aid needed being dependent on the type of press used. Washing the filter cake with Na SO solution removed additional non-toxic nitrogen which is desirable. In this washing step a 16.7% solution of Na SO was again used. This washing step removed an additional 15% of non-toxic nitrogen from the cake. After filtration the filter cake, which contains the ricin in combination with the Na SO may be dried and slurried with CCL, to separate the ricin by flotation. Separation of the ricin after a single precipitation and washing step is possible, but it is preferred to carry the process through an additional extraction and precipitation step. This is accomplished by slurrying the filter cake in three times its weight of water and the pH of the slurry is again brought to 3.8:.1 by means of 5% H The slurry is filtered and a second precipitation is brought about by adding Na SO solution.

Although pH control here is not wholly essential it is advantageous to bring the pH to approximate neutrality by adding 12% Na CO A precipitation time of 45 minutes was necessary to obtain complete removal of the toxin. In filtering out the precipitate, no filter aid was used and the filter cake was washed with Na SO solution on the filter whereby an additional amount of nontoxic nitrogen was removed from the cake. This washing was effective only the first time and repeated washings had little effect in removing further non-toxic nitrogen. The ricin-Na SO precipitate was dried at about 50 to 60 C. on a hot air tray dryer. The dried product was ground to pass a 40 mesh screen and agitated with 5 times its weight of CCl.;, which served the separate the ricin from the Na SO by flotation. After settling, the ricin was skimmed off the top. This reduced the Na SO content of the mixture from a previous 40 to 50% down to 15 to 18%. About 1 to 2% of nitrogen remained in the Na SO salt which could then be used for subsequent precipitations.

The final precipitation produced a particle size of 1-2 mu. On drying the wet cake, however, the ricin cemented together forming larger particles. These could not be broken down to their original size by ordinary grinding methods and since a very fine particle size was necessary in order that the product might be used as a toxic weapon, it was thought desirable to seek some method to prevent the agglomeration or cementing process that took place on drying. To attempt to affect this result, physical conditions prevailing under the precipitation process were changed. This included changing the temperature of precipitation and the rate of agitation. Other changes included precipitation with ony partial saturation of Na SO and the use of wetting and seeding agents. None of these expedients produced any significant improvement in particle size. Ordinary dry ball and hammer milling of the dried ricin produced considerable detoxifiiation perhaps due to the generation of excess heat. The use of CCl slurry plus the use of low temperature and low moisture content of the ricin reduced detoxification during ball milling. Spray drying proved to be an even better method of securing a reasonably small particle size.

Best results Were achieved by using a solution having about 20% solids, an inlet temperature of 150 C. and an atomizing air pressure of 150 to 180 psi. The particle size secured was 6 to 8 mu. The best means of securing a small particle size was by air grinding. This was carried out in an apparatus having a chamber with conical top and bottom. The material to be ground has been fed into this chamber and is withdrawn from the bottom and forced back into the center of the chamber tangentially through a venturi. Compressed air of about 100 psi. was fed to the venturi to provide the grinding force. The fines are drawn off the top and the large particles settle to the bottom to be recirculated and reground. This process produced particles having a mass median diameter of 2.5 to 3.5 mu. Numerous variations are possible in the several steps of the process commencing with the water extraction and precipitation which may be a single or multiple step. Although a single extraction step can be used, as indicated before, some process modifications are necessary for its successful operation on a plant scale.

Double extraction proved to be quite efiicien-t but additional steps beyond the second extraction step were not found necessary. The drawing is self-descriptive and shows the various steps of the process described. We claim: 1. In a method of preparing toxic ricin from castor beans comprising slurrying an expressed castor bean cake with water to remove the water soluble ricin and precipitating the ricin from the filtrate, the further steps which include slurrying the precipitate with CCl and separating the ricin by flotation. 2. A process in accordance with claim 1 in which the precipitate is dried prior to slurrying. References Cited in the file of this patent J. Gen. Physiol, vol. 32 (1948), pages 25-31. Non-Patent Citations The Terrorist's Favorite Weed: Castor Bean The Terrorist's Favorite Weed: Castor Bean The Castor bean plant (Ricinus communis) with its large bold, highly colored leaves is native to tropical Africa. In cold climates it is an annual, growing quickly, setting many seeds, and dying off in winter. In mild winter areas it is a long-lived perennial, sometimes reaching small tree size.

It has gone wild and naturalized in many places and is especially common in coastal areas. Each plant produces hundreds of the bean-like seeds and these seeds can remain viable for more than a decade. Castor bean is a Euphorbia (Spurge) family member and like many Euphorbias it is poisonous, has highly caustic sap, and produces extremely allergenic pollen. Before World War Two castor bean was not common in the US, grown mostly as an unusual foliage plant in a few gardens. But during the war there was a need for castor oil and the government encouraged farmers in the Midwest to start growing large acreage of it as an oil seed crop. The first year it was grown not much happened but by the end of the second season huge numbers of people living near the castor bean fields started getting hay fever and asthma. Castor bean pollen is an abundant and potent allergen. There is another more sinister use for castor bean. The mottled seeds of castor bean, which are about the size and shape of large pinto beans, contain two powerful poisons, the alkaloid ricinin and the toxalbumin ricin. Ricin, a white protein powder is a remarkably deadly cytotoxin.

The poison in the seeds is so strong that eating a single seed can kill a child. Animals, horses in particular, that eat the succulent leaves die from ricin poisoning. Ricin is even more toxic than strychnine and cyanides. Ricin also has the ability to accumulate in the body until a lethal dose is reached. Symptoms of ricin poisoning are stomachache, headache, fever, nausea and vomiting, bloody diarrhea, cold sweat, sleepiness, disorientation, shortage of breath, seizures, and death. Terrorists have long been enamored of castor bean and ricin. Modern day mad scientists can extract ricin from castor bean seeds. Just how poisonous is ricin? Ricin is one of the most poisonous naturally occurring substances known to man. As little as one milligram of ricin can kill an adult. Assassination Georgi Markov was a Bulgarian journalist who had spoken out against the Bulgarian government. While waiting for a bus near Waterloo Station in London, in 1978, Markov was murdered, stabbed in the leg with a poisoned umbrella. A perforated metallic pellet stuck in his leg was found to contain the deadly ricin toxin.

More recently it has been widely reported that Thomas C. Leahy, known by his neighbors as the “Mad Scientist,” was producing ricin in his Wisconsin basement. Leahy, a high school dropout and self-taught chemist, had also tried to grow anthrax. Ricin if inhaled or even touched can kill in a day or two. Luckily for us, Leahy is now serving seven years in state prison for shooting and wounding his 13-year-old stepson. Going Native Castor bean plant spreads quickly because it has many built-in advantages over native plants. A very robust grower, its leaves are poisonous even to predatory insects. Aphids that can safely feed on many other poisonous plants quickly die after sucking the juice of castor bean leaves. But castor bean has one disadvantage. It is completely easy to recognize and can then be killed by chopping it down or spraying it with herbicides. I have long advocated eradication of castor bean because it causes so many allergies. It would be wise to realize too, that not only is castor bean pollen allergenic, but it is also poisonous pollen. Exactly what the effects of breathing in poisonous pollen are we don’t know, but it cannot be good.

Given the deadly potential of this all too common weed for bio-terrorists, perhaps it is time we have our state and federal marijuana hunting exterminators, shift gears and change targets. They won’t have to look hard. In California Ricinus communis can be found growing lushly all along Highway 101. Copyright © 2017 Allergy Free Gardening None of the articles or photographs on this site are to be used without permission. For permission, please contact the webmaster. Ricin - AACC.org Home // ... // TDM and Toxicology Division // Toxin Library // Ricin Ricin Red bean is the jequirity bean and the brown bean is the castor bean. Both beans contain highly potent toxins. The jequirity bean is the source of abrin and the castor bean is the source of ricin. Both of these toxins are plant proteins known as phytotoxins and share many common properties. Both are composed of 2 peptide chains with the A chain inhibiting protein synthesis and the B chain binds to cell surface receptors. The source of ricin is the castor bean (technically not a bean but a seed).

The castor plant classification is: Kingdom: Plantae, Division: Magnoliophyta, Class: Magnoliopsida, Order: Malpighiales, Family: Euphorbiaceae, Subfamily: Acalyphoideae Tribe: Acalypheae, Subtribe: Ricininae, Genus: Ricinus, Species: R. communi. Castor plants are native to tropical Africa but are grown commercially to produce castor oil and grown extensively for its bold foliage as a decorative plant in parks and other public areas. The plant may be grown as an annual in colder regions reaching 2-3 meters in height or in warmer climates the height of small trees (12 meters). Castor seeds have been known for thousands of years and found with ancient Egyptian artifacts. Commercially nearly 1 million pounds of castor oil are produced each year with few accounts of toxicity. The use of castor seed oil in India has been documented since 2000 BC for use in lamps and in local medicine as a laxative, purgative, and cathartic in Unani, Ayurvedic and other ethnomedical systems.

Today it is used in the production of synthetic resins, plastics, fibres, paints, varnishes, and various chemicals including lubricants for heavy equipment, drying oils and plasticizers. Chemistry/Toxicology The castor seeds contain 20-90% castor oil composed of hydroxy fatty acids. Ricinoleic acid comprises about 90% of the total triglyceride fatty acids of castor oil. Ricin and other proteins in the seeds present the toxicological problem. Ricin has a molecular weight of 60-65 kDa composing 1-5% of the bean. Besides the ricin toxin, there's another compelling reason why this crop has fallen out of favor with U.S. growers. The shiny, beetle-shaped seeds contain powerful allergens. People who work with the off-white meal ground from castor beans may develop allergic reactions, such as hives or asthma. In severe cases, they may go into anaphylactic shock, which can be fatal. Chemistry was first elucidated by Stillmark in 1888 when he noted that the bean extract caused agglutination of red cells.

It is now know that this is another protein RCA(ricinus communis agglutinin). Ricin is a potent cytotoxin but only a weak hemagglutinin. The figure of the ricin structure is a drawing modeled from X-ray crystallography data. The upper right half, the dotted ribbon, is the A chain, and the lower left half, the solid ribbon, is the B chain. The A chain (or RTA)is a 267-amino acid globular protein. It has 8 alpha helices and 8 beta sheets. The substrate binding site is the cleft marked by the substrate adenine ring. The B chain (or RTB) is a 262-amino acid protein that is shaped like a barbell. It has a binding site for galactose at each end, (depicted by lactose rings). These two sites allow hydrogen bonding to specific membrane sugars (galactose and N-acetyl galactosamine). A disulfide bridge (-S-S-) joins RTA with RTB. The B chain binds to galactose-containing glycoproteins and glycolipids expressed on t the surface of cells.

The A chain can then gain access to the cell and inhibits protein synthesis by irreversible inactivating ribosomes through removal of a single adenine residue from RNA loop contained within the 60S subunit. This process prevents chain elongation and leads to cell death. This general mechanism is characteristic of a broad class of toxins such as diphtheria, botulinum and anthrax. The RCA toxin causes agglutination and subsequent hemolysis. Clinical toxicology cases are from ingestions of the bean and none have been reported from the purified ricin although this was major concern a few years ago. The most famous death was Georgi Markov in London in 1978. Markov was attacked with a specially engineered weapon disguised as an umbrella which implanted a ricin-containing pellet into his body. Exposure Most human exposures have occurred from oral ingestion of the seeds. The clinical consequences depended on the concentration of ricin in the seeds and the how well the seeds were chewed. Although death can occur from as little as one seed, ricin does have poor absorption and ingestions of multiple seeds in small children have not been fatal. Ricin injection can be more fatal as evidence by the Markov case.

Symptoms even with injection are delayed with nausea and vomiting after 15-24 hours. Death occurred 24-36 hours after injection. Of greater concern from a biological weapons viewpoint is exposure by inhalation. Symptoms again are delayed for 8-24 hours but death occurs from 36-48 hours. The effectiveness of the exposure depends on the particle size of the ricin preparation. The smaller particles reach the small alveoli and are absorbed. It should be noted that sophisticated grinding apparatus is needed to produce the “weapons grade” ricin powders. In experimental animals death (36-48 hrs) from inhalation was due to massive inflammatory response to ricin leading to respiratory insufficiency and death. The LD50 for the inhalation route is 3-5 microgram per kilogram using rodent models as compared to the oral LD50 of 20 mg/kg Additional primate data substantiated an approximate LD50 of 10 microgram per kilogram. Although most workers in castor oil plants are never exposed to ricin many toxic symptoms from other highly antigenic proteins found in the bean.

References Franz, DR and NK Jaax, "Ricin Toxin" Chapter 32, Medical Aspects of Chemical and Biological Warfare, Office of the Surgeon General, Department of the Army, 1999. Audi J, Belson M, Patel M, Schier J, Osterloh J. Ricin poisoning: a comprehensive review. JAMA 2005;294:2342-51. Bradberry SM, Dickers KJ, Rice P, Griffiths GD, Vale JA. Ricin poisoning. Toxicol Rev 2003;22:65-70. Ler SG, Lee FK, Gopalakrishnakone P. Trends in detection of warfare agents. Detection methods for ricin, staphylococcal enterotoxin B and T-2 toxin. J Chromatogr A 2006;1133:1-12. Olsnes S. The history of ricin, abrin and related toxins. Toxicon 2004;44:361-70. Hedge, R and S.K.

Podder, Studies on the variants of the protein toxins ricin and abrin, Eur. J. Biochem. 1991; 204, 155-164. Spivak L, Hendrickson RG. Ricin. Crit Care Clin 2005;21:815-24, viii.

Question: What potent toxin is extracted from the castor bean?
Answer: Ricin