Is that mad cow

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You are correct! Creutzfeldt–Jakob Disease is Mad Cow Disease. ChaCha! [ Source: ]
More Answers to “Is that mad cow
Is mad cow disease the same thing as rabies
No, it’s only called mad cow disease because it affects a cow’s nervous system, causing a cow to act strangely and lose control of its ability to do normal things, such as walk. The cow does not enrage.
What is the mad cow disease?
Mad cow disease affects the cow’s nervous system. It causes the cow to act differently. The cow loses control of its ability to walk as well as other normal things. You can find more information here:…
How do you get mad cow disease?
Although it is said that you cannot get mad cow disease from a mad cow this is somewhat true. However there has been link between the rare brain condition that does have an affect with people to be one in the same with a mad cow. Look here …

Related Questions Answered on Y!Answers

Can you get Mad Cow Disease from Gummy Bears?
Q: I used to be a fan of Jello until I read how it was made – boiling cow bones until they dissolve. I can’t even eat Jello anymore considering the beef industry practice of trying to kill the beef eaters.I realize that Gummy Bears are made from Gelatin. The same stuff Jello is made up of.Can I get Mad Cow from Gummy Bears? I’m guessing YES, so I’ll have to drop that as a snack too.
A: The answer is – YES.You can acquire Mad Cow Disease from eating Gummy Bears.Gummy Bears were originally created in Germany in 1922. Since then, they have used animal derived gelatin which is made by boiling cow bones to extract the core elements.Since boiling / cooking does not destroy the Mad Cow Disease proteins – it is possible to get Mad Cow from eating anything created by animal by-products – this includes gelatin.So, if you are concerned with your health, you should avoid eating Jello and Gummy Bears or any food/candies made with gelatin since the source is not strictly controlled.
Is Mad Cow Disease still in the deer population in any State?
Q: I read that Mad Cow Disease was in the deer population of New Mexico at one point.Is this still a problem? I live in Texas.And how do you know if the deer you shot has the disease?
A: it’s chronic wasting disease(CWD), not mad cow, similar, but chronic wasting disease is unique to deer, moose and elk, but it can be transfered to is still out there, but you should be safe, the disease seems to be on the northwestern border of texas, but you still should be safe anywhere’s else.the only ways to figure out if a deer has CWD is to watch the animal before shooting it, in most cases it’ll look disoriented(dizzy, off balance), unafraid of people, trying to keep away from the herd, this would be weird in texas right?very bad health(thin, obvious bones on the ribs, hips and face), if you shoot a deer and it has a smell of rotting meat, that is a definite sign that it has CWD, since the disease literally infects the whole body and starts destroying it.also, if the deer isn’t showing any of these signs, I wouldn’t be worried about it.the other way is to test the brain of a dead deer for the disease, you can bring it to a DNR and they’ll send it off a sample to be tested, you can request a result from the DNR when it comes in, shouldn’t be long, but is kind of annoying since you may have the deer completely butchered and find out that it’s diseased, if you can, I would freeze it in a freezer whole(gutted of course) before wasting all that effort for nothing, I believe you can ask for a new tag since you were not able to keep the animal, but I may be wrong’s a map that shows the locations and type of infections back in 2006, shouldn’t be much different today:’s a video that shows a deer that’s obviously infected with CWD, it’s not rabid.
How could people get Mad Cow Disease?
Q: How could people get Mad Cow Disease? The theory I’ve heard is that people could get Mad Cow Disease from proteins that are misfolded. I thought in the digestive track proteins are split into amino acids before being absorbed into the bloodstream, so shouldn’t the shape of the protein be irrelevent?
A: Both classic and variant CJD belong to a broad group of human and animal diseases known as transmissible spongiform encephalopathies (TSEs). The name derives from the spongy holes, visible under a microscope, that develop in affected brain tissue.TSEs in humansOne of the oldest known human TSEs is kuru. Found only in a remote New Guinea tribe, kuru reached epidemic proportions in the 1950s and 1960s. How the disease originated isn’t clear, but scientists know that it spread when tribe members ritualistically consumed the brains of dead relatives.Other human TSEs include Gerstmann-Straussler-Scheinker disease and fatal familial insomnia — hereditary diseases so rare they occur in just a few families.TSEs in animalsThe most widespread TSE in animals is scrapie, a disease that has affected sheep and goats since the mid-18th century. Infected animals become agitated, attempt to rub off their wool by scraping against trees and posts, and usually die a few months after symptoms appear. Many experts believe that British cattle developed mad cow disease after being fed the remains of scrapie-infected sheep.Other animals affected by TSEs include domestic and exotic cats (feline spongiform encephalopathy); mule deer, white-tailed deer, black-tailed deer and elk (chronic wasting disease); and mink (transmissible mink encephalopathy).The origin of TSEsThe cause of TSEs eluded scientists for centuries. But in the early 1980s, Stanley Prusiner, a researcher at the University of California at San Francisco, suggested that the infective agent in TSEs wasn’t a virus or any other known pathogen. Instead, he blamed an infectious protein, which he called a prion — short for proteinaceous infectious particle. This was a daring leap because proteins don’t contain RNA, the genetic material that allows viruses and bacteria to reproduce. But today, the link between prions and TSEs is widely accepted.The nature of prionsPrions are proteins that occur naturally in the brains of animals and people. Normally, these proteins are harmless, but when they’re misshapen they can cause devastating illnesses. The difference lies in the way the proteins are folded.All proteins start out as loose strings of amino acids. But proteins can’t perform their intended function until the amino acids fold into a specific three-dimensional shape. The shape a particular protein assumes is determined by the sequence of its amino acids. Most proteins fold spontaneously during or just after they’re synthesized inside cells, the entire process lasting only a few tenths of a millisecond.Protein folding isn’t foolproof, however, and many proteins made by the body aren’t usable. The rejects are sent to a kind of recycling center, where the amino acid chains are disassembled and the amino acids prepared for reuse. Normally, this system works well. But as people age, the recycling process may stop working efficiently. As a result, misfolded proteins begin to accumulate in deposits that can cause serious problems. This seems to be what happens in Alzheimer’s disease, for example.But prions go one step further. Not only do they misfold, they also enter brain cells and force normal proteins to misfold as well. When the infected cells die, prions are released into normal tissue and go on to infect more cells. Eventually, large clusters of cells die, leaving the brain riddled with holes.Unlike any other known protein, prions are infectious. When misfolded proteins are transmitted to people or animals, they begin to transform healthy brain cells into abnormal ones, although signs and symptoms of disease may not appear for years.Prions also seem capable of crossing species’ barriers, jumping, for example, from sheep to cows to humans. Although infection may occur more readily when proteins have the same amino acid sequence and exist within a single species, evidence is strong that prions can move from one species to another.To make matters worse, prions are nearly indestructible. They’re impervious to radiation, washing, boiling and the intense heat of autoclaves used to sterilize surgical instruments. Unlike many harmful bacteria, prions aren’t destroyed by cooking or by the strong juices produced in your stomach.How CJD is transmittedMost people with classic CJD develop the disease for no apparent reason. CJD that occurs without explanation is termed spontaneous or sporadic CJD and accounts for the great majority of all cases.Researchers have been able to identify some causes of CJD, however, including: * Heredity. In the United States, about 5 percent to 10 percent of people with CJD have a family history of the disease or test positive for a genetic mutation associated with CJD. * Certain medical procedures. So far, classic CJD hasn’t been linked to tainted beef. But a small number of people have developed the disease after being exposed to infected human tissue as a result of medical procedures (iatrogenic CJD), such as cornea and skin transplants and grafts of dura mater, the membrane that covers the brain. Some adults have developed CJD decades after receiving injections of human growth hormone (HGH). Traditionally, HGH has been used to treat children who fail to grow normally, but in recent years it also has become popular as an anti-aging therapy. Before the 1980s, when a genetically engineered version of the hormone became available, HGH was derived from human pituitary glands. * Exposure to contaminated medical instruments. Because rogue prions aren’t affected by standard sterilization methods including heat, radiation, alcohol, benzene and formaldehyde, instruments used in some types of brain surgery can harbor small bits of infected tissue, even after undergoing stringent cleaning procedures.How vCJD is transmittedTo date, vCJD has been linked primarily to the consumption of beef infected with mad cow disease. The parts of meat most likely to harbor infection include: * Bone marrow * Brain * Spinal cord * Nerves attached to the brain, eyes, tonsils and spinal cord * Small intestineHot dogs, ground meat and sausages are especially likely to contain contaminated tissues, whereas milk and other dairy products haven’t been implicated in vCJD.Studies have also shown that vCJD can spread through blood transfusions, even if the infected donor has no signs or symptoms of the disease. TSEs in animals appear to spread through close contact; one study suggests infected prions may spread through animal urine. But current evidence doesn’t suggest that either CJD or vCJD can be transmitted from one person to another through social or sexual contact.
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