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Jeff Sutherland

Twice the Energy with Half the Stress

Researchers use Rife cancer germ to produce enzyme that degrades Mad Cow disease prions

The EPA has chosen not to regulate Bacillus licheniformus, which was recently identified by British researchers as the Rife “cancer germ” through DNA sequencing of multiple pleomorphic forms of this organism. This organism appears to be a mutagen and tumor promoter, is sold in many probiotic nutritional products, and is extremely hazardous. Eliminating this organism is the first step in dealing with any form of cancer and it appears in virtually all cancer patients. This is documented extensively in my archives.

Fortunately, the researchers have isolated the enzyme produced by Bacillus licheniformus that degrades Mad Cow prions. Unfortunately, the ignorant may promote putting Bacillus licheniformus in animal feed and expose us to signficantly increased risk of cancer. I strongly recommend you avoid any food that may be contaminated by Baccilus licheniformus. I’ve found this in animal meats, certain oils, as well as in probiotic supplements. Fortunately, in the case of some probiotics, they list it on the package as an ingredient, so the knowledgeable can avoid this hazard in some cases.

It would be interesting to followup these researchers over the years as they may have infected themselves with Bacillus Licheniformus and be at high risk of developing cancer.

Enzymatic degradation of prion protein in brain stem from infected cattle and sheep

Langeveld JP, Wang JJ, Van de Wiel DF, Shih GC, Garssen GJ, Bossers A, Shih JC.

J Infect Dis. 2003 Dec 1;188(11):1782-9.

Prions-infectious agents involved in transmissible spongiform encephalopathies-normally survive proteolytic and mild protein-destructive processes. Using bacterial keratinase produced by Bacillus licheniformis strain PWD-1, we tested conditions to accomplish the full degradation of prion protein (PrP) in brain-stem tissue from animals with bovine spongiform encephalopathy and scrapie. The detection of PrPSc, the disease-associated isoform of PrP, in homogenates was done by Western blotting and various antibodies. The results indicated that only in the presence of detergents did heat pretreatment at >100 degrees C allow the extensive enzymatic breakdown of PrPSc to a state where it is immunochemically undetectable. Proteinase K and 2 other subtilisin proteases, but not trypsin and pepsin, were also effective. This enzymatic process could lead to the development of a method for the decontamination of medical and laboratory equipment. The ultimate effectiveness of this method of prion inactivation has to be tested in mouse bioassays.

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