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Scientists Study Natural Enzymes To Clear Contaminent Caused Diseases
Enzyme treatments are being probed by conventional
research scientists. They are proving us right.
Scientists are bringing out an enzyme they call
keratinase, but we call Karribatakoe.
Ingesting our herbs with spirulina provides materials and instructions for the body to produce enzymes. Two of these enzymes are discussed below.
Are doctors and pharmaceutical companies opposed to enzyme therapy because it clears up the problems, because they only want to promote artificial drugs that leave the underlying cause to continue?
Names of the Grazoph products and the word grazoph itself are
from Taomarik, who lives far away. It is said there is nothing like
Grazoph on any planet around, for 700 light years distance. The word
grazoph implies the use of spirulina in these formulas.
Discovery of
Karribatakoe
Orange enzyme produced by the Heart
Study: Enzyme can degrade mad cow prion
Monday, 5-Jan-2004 4:50PM EST
Copyright 2004 by United Press International
Jan. 5 (UPI) -- North Carolina researchers
have shown that an enzyme can fully degrade the prion -- or protein
particle -- believed responsible for mad cow disease.
Research by North Carolina State University
and scientists from the Netherlands and BioResource International, have
shown that, under proper conditions, the enzyme can fully degrade the
prion believed to be the cause of bovine spongiform encephalopathy, as
well as the human and sheep versions, called Creutzfeldt-Jakob disease
and scrapie.
The research, published in the Journal of
Infectious Diseases, tested the effects of a bacterial enzyme
keratinase on brain tissues from cows with BSE and sheep with scrapie.
When the tissue was pretreated and in the presence of a detergent, the
enzyme fully degraded the prion, rendering it undetectable.
"Our work has been done in vitro, or in test
tubes, and we've reduced the prion to undetectable levels," said Dr.
Jason Shih, professor of biotechnology and poultry science at North
Carolina State. "Our work with mice will show whether these
undetectable levels of prion are indeed non-infectious."
The researchers plan a two-year study,
funded with $190,000 from the National Cattleman's Beef Association, to
test the effectiveness of the enzyme on the treated BSE prions in mice.
Discovery of Dtwel Makandtexdopho
not-blue enzyme produced by the lungs
From The Japan Times May 25, 2001
Japanese team finds enzyme that stops Alzheimer's disease
Researchers at an
affiliate of a Japanese government-backed research
institute said they have discovered that an enzyme in the brain plays a
key role in preventing or delaying the development of Alzheimer's
disease, the U.S. magazine Science reported Friday. News of the
discovery comes two days after the announcement that a team of
researchers led by a Keio University professor has found a gene that
prevents brain cells from deteriorating from Alzheimer's.
Alzheimer's, a neurodegenerative disease, kills neuronal cells and
shrinks the brain, causing dementia. A research team led by Takaomi
Saido of the Saitama Prefecture-based Riken Brain Science Institute, an
affiliate of the Institute of Physical and Chemical Research,
discovered through experiments on mice that the enzyme Neprilysin
"cleans up" Beta-amyloid, a substance that destroys brain cells.
This mechanism is considered to be crucial in preventing Alzheimer's or
delaying its symptoms, as Neprilysin is known to decompose accumulated
Beta-amyloid.
The experiments involved the use of normal mice and those that had been
genetically modified so that they were unable to produce Neprilysin.
The team found that the decomposition capability of the normal mice
was, at maximum, double that of those without Neprilysin. Mice that had
inherited a genetic abnormality from only one parent also showed a
lower decomposition capability than normal mice.
Most Alzheimer's patients have roughly the same amount of Beta-amyloid
in the brain as healthy people, and it is thus not known how the
disease starts to develop. The discovery suggests, however, that some
people inherently carry less active Neprilysin and that these people
develop the disease as they grow older, with their clean-up mechanism
becoming inefficient, the team said. The team expects that genetic
therapy will be able to be applied to patients whose Neprilysin has
become less active, should studies on the enzyme at the genetic level
proceed
The Japan Times: May 25, 2001 (C) All rights reserved
Thanks to
Claire Johnstone (clairejohnstone@libertysurf.co.uk)
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