Re: Colloidal silver generator?

John Woodgate wrote:

> Mike Monett <no@xxxxxxxx> wrote

>> Hemoglobin is also a metalloprotein, but it transfers oxygen
>> without combining with it, which would be fatal.

> I think you should reconsider that. Find out why arterial blood is
> a different colour from venous blood.

The hemoglobin metalloprotein is a marvel of exquisite design. It
has to transfer oxygen but it cannot bind tightly since it has to
release it when needed. Here's the problem definition and solution:

"Oxygen binds to the iron ion tightly, and if two heme molecules
come together in the presence of oxygen the iron atoms will
oxidize and irreversibly bind to the oxygen."

"This irreversible binding would not be of use in the hemoglobin
molecule because oxygen needs to be released in the tissues. The
globin chain prevents this irreversible binding by folding the
protein around the heme molecule, creating a pocket to isolate the
heme molecule from other heme molecules (Perutz, 1978)."

"Therefore, the globin molecules allow the iron atom to form loose
bonds with the oxygen, and therefore, the ability to bind to
oxygen and then release it into the tissues without becoming
permanently oxidized in the process."

http://www.bio.davidson.edu/Courses/Molbio/MolStudents/spring2005/Heiner/hemoglobin.html

Here is a marvellous animation showing how hemoglobin shifts
position as it picks up oxygen:

"Hemoglobin is a remarkable molecular machine that uses motion and
small structural changes to regulate its action. Oxygen binding at
the four heme sites in hemoglobin does not happen simultaneously.
Once the first heme binds oxygen, it introduces small changes in
the structure of the corresponding protein chain. These changes
nudge the neighboring chains into a different shape, making them
bind oxygen more easily. Thus, it is difficult to add the first
oxygen molecule, but binding the second, third and fourth oxygen
molecules gets progressively easier and easier. This provides a
great advantage in hemoglobin function. When blood is in the
lungs, where oxygen is plentiful, oxygen easily binds to the first
subunit and then quickly fills up the remaining ones. Then, as
blood circulates through the body, the oxygen level drops while
that of carbon dioxide increases. In this environment, hemoglobin
releases its bound oxygen. As soon as the first oxygen molecule
drops off, the protein starts changing its shape. This prompts the
remaining three oxygens to be quickly released. In this way,
hemoglobin picks up the largest possible load of oxygen in the
lungs, and delivers all of it where and when needed."

"In this animated figure, the heme group of one subunit, shown in
the little circular window, is kept in one place so that you can
see how the protein moves around it when oxygen binds. The oxygen
molecule is shown in blue green. As it binds to the iron atom in
the center of the heme, it pulls a histidine amino acid upwards on
the bottom side of the heme. This shifts the position of an entire
alpha helix, shown here in orange below the heme. This motion is
propagated throughout the protein chain and on to the other
chains, ultimately causing the large rocking motion of the two
subunits shown in blue."

http://www.rcsb.org/pdb/molecules/pdb41_2.html

> But that's an aside. If it's silver ions that have the therapeutic
> effect, who go to the trouble of making 'colloidal silver'? Why
> not just make a very dilute solution of a salt of silver and a
> weak acid? That gets you the Ag+ and OH- ions you need.

> Regards, John Woodgate,

Hi John,

You are right - making good quality Ag(+) is a real pain in the
neck. However, you don't need the OH(-) ions, as my double chamber
cs generator demonstrates:

http://escribe.com/health/thesilverlist/m78983.html

The plain ion is needed since silver compounds have significantly
poorer biological effect. For example, silver nitrate has a standard
concentration of 0.5% which translates to 3180 ppm of silver:

http://www.burnsurgery.org/Modules/silver/section3.htm

A simple ionic cs solution of 10 ppm can easily be made with a 3
nines generator and does the same job without risk of tissue damage
or staining.

Mild Silver Protein compounds (MSP) are virtually useless. These are
the products where the FDA complained they discovered bacteria
growing in the gel. They have such high silver concentration there
is a real risk of Argyria.

Other products containing silver citrate are available. Here's one
with a concentration of 100ppm:

"Silver 100 with Opti-Silver utilizes an entirely new approach to
silver ion delivery. It is designed to overcome all the
limitations of other forms of silver. It utilizes a proprietary
method of complexing silver ions with a special form of citrate
that acts as the stabilizer and delivery vehicle."

http://www.silver100.com/details.html

However, the time/kill study shows it has very poor performance.
Scroll down to "1) Antibacterial Time-Kill Study":

http://www.earthbornproducts.com/product.htm

This is even worse than Steve Quinto's results with Mesosilver:

http://tinyurl.com/3qb4v

So the shortcuts don't work and can be harmful.

> The other Mark implies that it never reaches the stomach but forms
> purple metalloproteins in the mouth. It's plausible.

There's only one Mark - Mark Jones.

There are several Mikes - I'm the one who has been posting the
information on how to make cs, the silver electrolysis equations,
solubility of silver hydroxide, the Faraday calculations, Fred
Peschel's metalloproteins, Steve Quinto's results with Mesosilver,
Frank Key's misinformation, and so on.

Mike Monett
.

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