Mercury, Lead, & Arsenic DETOX with Copper, Zinc & Selenium

When people are mercury toxic, very often they have other problems, too: mold, Lyme, parasites*. Copper fixes all of these problems. Here’s how to detox:

Simply take copper, zinc, Vitamin C, selenium, colloidal gold, and blueberry, as indicated on our protocol guide here:

The Copper Revolution Protocol:

The Copper Revolution Protocol, June, 2024

Why does it work?

All three, copper, zinc, and selenium, are needed to make metallothionein, a copper/zinc/selenium enzyme. Metallothionein detoxes mercury, lead, arsenic, and other heavy metals.

https://en.wikipedia.org/wiki/Metallothionein

“MTs have the capacity to bind both physiological (such as zinc, copper, selenium) and xenobiotic (such as cadmium, mercury, silver, arsenic) heavy metals through the thiol group of its cysteine residues”

Cysteine is a common amino acid, present in most meat, and beef is a good source high in cysteine.

(Metallothionein is the same enzyme that “zinc makes” which detoxes and lowers copper and can create a “zinc induced” copper deficiency. At 15:1 zinc to copper, you will induce a copper deficiency. This is why you have to balance the zinc and copper more at the 2:1 or 5:1 ratio of zinc to copper.

How do you know if you are mercury toxic?

If you have had mercury fillings. Shots. Exposure to fluorescent light bulbs, especially broken bulbs.

Are you sensitive to sulfur or high sulfur foods like garlic, eggs, or spinach? Symptoms would include worsening mercury toxicity symptoms such as mental confusion. That usually indicates mercury toxicity.

After you clear out most of your mercury, start with eating spinach. Then eggs, then garlic, then try an MSM Sulfur supplement. If you can tolerate those foods again, that is your test you are on track. In fact, try to push it.

Sulfur is “intolerable” because it is a GREAT detoxer, it even helps mercury detox. But not good enough on its own for mercury, and you need those other nutrients more, and first. So add MSM sulfur to the protocol of things you are taking, last.

If copper sulfate has too much sulfur to tolerate, or if you suspect that the sulfur part of it is causing allergic reactions, it is perfectly fine to take copper glycinate for the first few months, 2-3 months, until sulfur can be tolerated. We took copper glycinate for our first 3 years on high copper, only because we did not know about copper sulfate, which is far far far cheaper.

There is very very little sulfate in copper sulfate–only about two times the amount of copper. So 10 mg of copper sulfate contains only about 20 mg of sulfate. In context, a teaspoon of MSM sulfur supplement contains 8000 mg of sulfate.

As always, do not forget to take ascorbic acid, Vitamin C, with copper on the protocol. About 1000 mg to 2000 mg when starting.

We believe a person has to work up to about 10 mg of copper per day, and stay at that dose for about a month, for the body to start making metallothioneins. After that time, increasing copper to around 20-30 mg, slowly again, appears to be a very effective dose. Many people in our forum also report great results from 50 mg up to 200 mg of copper, although doses above 100 mg are often only done on a temporary basis.

Some people like more evidence and research on what Metallothioneins are and do. See this link:

Copper and Zinc Metallothioneins for Detoxing & Longevity

Some people ask if they need to remove their mercury fillings first. No, you do not. That is the advice from a different mercury detox protocol that does not work very well. In fact, removing mercury fillings, before your body is healthy enough to detox mercury, is doing things backwards, as if you are already suffering from mercury, and then get increased exposure to mercury right when you are deficient in copper, things can go very bad very quickly. Get copper levels up first, then remove the fillings if you think you need to.

Some people ask how tightly metallothioneins bind to mercury, and if they cause redistribution. Metallothioneings bind very tightly to mercury, and they can’t even be digested or degraded in the digestive tract. Once mercury is bound and trapped into metallothioneins, it can’t get back out of that, and it is headed for excretion out of the body.

Here’s what Claude.AI says:

The mercury-MT complexes have some of the longest and most stable half-lives of any metal-MT combinations, due to mercury’s extremely strong binding affinity for the thiol groups in MT.

Definitely Known:

1. Mercury-MT bonds are among the strongest metal-thiolate bonds
2. Mercury has higher binding affinity than copper, zinc, or cadmium
3. This makes mercury-MT complexes very stable
4. The strong binding helps prevent mercury from being released

Less Certain (using uncertain language):

• The exact half-life numbers might vary by conditions
• The body might handle these complexes differently than other metal-MTs
• Different routes of excretion might be involved
• Environmental factors could affect stability
• The presence of other metals might influence the stability

I should acknowledge that while I know mercury-MT complexes are very stable, I don’t feel confident citing specific half-life numbers without verification. This stability is likely why MTs are so important in mercury detoxification.

===== More from Claude.AI:=====

Let’s explore the unique properties of metallothioneins (MTs) that make them resistant to digestion:

1. Structural Features:

• Extremely high cysteine content (up to 30% of amino acids)
• These cysteines form multiple sulfur-metal bonds
• The protein folds into a unique “dumbbell” shape
• Has two metal-binding domains (α and β domains)
• Forms multiple metal-thiolate clusters
• These clusters create a very tight, stable structure

1. Metal-Binding Properties:

• Can bind 7-12 metal ions per molecule
• Forms very stable metal-thiol bonds
• The metal binding actually stabilizes the protein structure
• Different metals bind with different affinities:
• Strongest: Mercury, Cadmium
• Strong: Copper, Zinc
• Less Strong: Iron, other metals

1. Resistance Mechanisms:

• The metal-thiolate clusters make the protein very compact
• Multiple cross-links make it harder for digestive enzymes to access cleavage sites
• The tight folding protects peptide bonds from proteases
• The structure becomes more stable when metals are bound
• Metal binding can make the protein even more resistant to degradation

1. Evolutionary Significance:

• This resistance to degradation appears purposeful
• Allows for safe transport of toxic metals out of the body
• Prevents reabsorption of dangerous metals
• May explain why copper bound to MTs isn’t readily reabsorbed

More on Selenium:

Mercury Detox using the Selenium Method:

https://www.facebook.com/groups/341263176792506/

https://prevent-alzheimers-autism-stroke.blogspot.com/2019/07/mercury-detox-using-selenium-method.html