Re: [rife-list] Prions & freq? Ultrasound breakage.

[Guest guest]

Hi everybody,

Del has posted something very interesting about prion research. There is a

process called Protein Misfolding Cyclic Amplification, it is done with

ultrasound. It can be used in labs to test tissues for the misfolded prion. It

literally causes a misfolded prion to create more of the same, in other words,

its numbers are amplified. The ultrasound causes a piece of misfolded protein

to break off, which then attaches to good prion and converts it to bad. I took

some notes about the process last summer...they are copied below. From what I

have seen so far, it is not a frequency-specific process (but am not certain on

that). What does seem relevant is that a shock-type wave is necessary for the

phenomenon. This is why I have NOT followed up on using freqs for the prion

problem. It just may not be appropriate, unless someone can find out what power

levels and waveform would be effective. That would take some serious lab work.

There is also a very nice article about this ultrasound process, I have a copy

of it but cannot include due to copyright restrictions. It was perhaps the

first article (or one of the first) announcing this process. There is a good

diagram on the first page that shows how it happens (a picture is worth a

thousand words!). The citation is:

Saborio, a P, et al. Sensitive detection of pathological prion proteinby

cyclic amplification of protein misfolding. Nature, vol. 411, p. 810-813, 14

June 2001.

Does anyone remember the guy Mark Purdey, he is in England and has done so much

work on mad cow disease and the related human form? And remember how he

insisted that people in earthquake-prone areas seemed more susceptible to the

condition? (Shock waves). And he also talked about the pesticides and how it

upsets the mineral balance. Well, I have seen some material from a different

scientific source that seems to indicate that the tendency for prion midfolding

is enhanced by the presence of inorganic, crystalline-like form of certain

essential minerals (as opposed to organic, healthy, bio-available forms of those

minerals). I would have to dig to find that material, just wanted to mention

it, because maybe Mark Purdey is onto more than anyone ever thought.

Thanks Del, for posting this along with the cite! :-)

Best wishes, Char

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from http://bse.airtime.co.uk/PA613.html

June 13/01

AP/Reuters/Agence France Presse English

Scientists, according to these stories, have developed a method to rapidly

culture large amounts of the infectious agent blamed for mad cow disease, a

development they say could improve testing and research into the malady that

has threatened European livestock and consumers.

The stories say that researchers at the Serono Pharmaceutical Research

Institute in Switzerland said they placed prions from infected hamster

brains in a dish with normal hamster brain proteins. More than 97 percent of

the normal proteins were converted to prion-shaped proteins using an

ultrasound technique.

-----------------------------

PROTEIN MISFOLDING CYCLIC AMPLIFICATION The procedure is termed Protein

Misfolding Cyclic Amplification (PMCA). Minute samples of abnormal prion

protein (PrPsc) were taken from the brains of scrapie infected hamsters,a nd

mixed with large excess amounts of normal prion protein (PrPc) from

disease-free hamsters. This resulted in a rapid conversion of the normal

prion protein into many aggregates of the abnormal prion protein. The

aggregates were then treated with ultrasound. This cycle of amplification

can be repeated many times within a day in a laboratory to produce

quantities of the abnormal prion protein which are several hundred times

greater than is currently available in the brain tissue of dead animalso r

humans.

----- Original Message -----

From: delgcrow

Another abstract " swiped " :

Biochem Biophys Res Commun. 2005 Jan 14;326(2):339-43.

·Breakage of PrP aggregates is essential for efficient autocatalytic

propagation of misfolded prion protein.