[compost_tea] Re: Scientists Discover Enzyme Degrades Mad Cow Disease Prion (fwd)

From: longbranchranch <longbranchranch_at_yahoo.com>
Date: Thu, 08 Jan 2004 14:28:18 -0000

---Elaine this is a very interesting discovery but not the first. Mark
Purde a organic dairy farmer from England launched research some years
ago the showed the common denomanetor in the mad cow out breaks was
verry low copper and high manganese. The manganese replaces copper in
a would be normal prion, making a rouge prion that destroying the
nervious system. Some of the causes is minning and organophosfate
insecticide. This is poured down the backs of cattle to kill worms.
The simple eradication would be neutrition (proper mineral ballance)
and of cource ban of all chemical insecticides and herbacides. Why
havn't we heard of this? One guess, government and the like of Dow
chemistry.
Jimmy Muse
PS: I will forward mr Purde web paige on reguest.



In compost_tea_at_yahoogroups.com, "dakesian1" <dakesian_at_s...> wrote:
> "Phew" is right! Thank God someone found a possible solution. That
> is GREAT news!
>
> Rick
>
> --- In compost_tea_at_yahoogroups.com, soilfoodweb_at_a... wrote:
> > Look at this! Keratinase is indicated as the enzyme that
> decomposes prions! Good old Bacillus licheniformis! This is good
> news, because guess what compost abounds in? If you use hair,
> feathers, fungal hyphae and other similar materials in the compost,
> you are enhancing keratinase! So, compost is a good way to deal
> with suspect materials. Phew!
> >
> > So, what concentrations needed to make sure 100% reduction? Well,
> that needs to be figured out.
> >
> > Elaine
> >
> >
> > In a message dated 1/7/2004 1:31:30 PM Eastern Standard Time,
> marilyn_at_D... writes:
> >
> > > Enzymatic Degradation of Prion Protein in Brain Stem from
> Infected Cattle and Sheep"
> > > Authors: Jan P.M. Langeveld, Dick F.M. Van de Wiel, G. Jan
> Garssen and Alex Bossers, Central Institute for Animal Disease
> Control, Lelystad, The Netherlands; Jeng-Jie Wang and Giles Shih,
> BioResource International; and Jason C.H. Shih, Dept of Poultry
> Science, North Carolina State University
> > > Published: Dec. 1, 2003, edition of The Journal of Infectious
> Diseases
> > >
> > > Abstract: 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 PrP^Sc, 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°C allow the extensive
> enzymatic breakdown of PrP^Sc 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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Received on Thu Jan 08 2004 - 10:41:43 EST

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