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Treating mercury toxicity with emeramide 
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Beitrag Treating mercury toxicity with emeramide
Treating mercury toxicity with emeramide


Boyd Haley, Ph.D., is a chemist specializing in the development of chemicals to chelate toxic metals, both from the environment and the human body. I had the opportunity to interview Haley (below) at the 2018 Academy of Comprehensive Integrative Medicine (ACIM) conference in Orlando.To get more news about Emeramide for sale, you can visit fandachem.com official website.

Haley has a Ph.D. in chemistry and biochemistry and conducted research funded by the National Institutes of Health (NIH) for 25 years at the University of Wyoming and at the University of Kentucky. Early in his career, he developed a biochemical detection system called nucleotide photoaffinity labeling and has published studies on its usage.1 Haley explains:
I took ATP and made it radioactive, which isn't a big feat. But then I attached to that a molecule that would explode when it hit a photon of light. When it exploded, it made a very reactive intermediate that had a half-life of something like 10-12 or 10-13 seconds.
If ATP was bound to a protein, such as sodium potassium ATP [and] ... you hit it with light, it would form a covalent bond at the binding site of ATP on the enzyme it was interacting with ...

You could use these kinds of probes to see the difference between the ATP, guanosine diphosphate (GDP), cyclic adenosine monophosphate (AMP) and nicotinamide adenine dinucleotide (NADH) — all these binding proteins, to see how the energetics of the cell was changing.
He later took a position with the Alzheimer's Center, a research center for Alzheimer's disease, where he collaborated with a former graduate student of his. The NIH funded their research for five years, which used Haley's technology to assess the differences of ATP, GDP and cyclic AMP binding proteins in normal brains versus those with Alzheimer's disease.

"There were dramatic differences," he says. For example, the enzyme creatine kinase, which is a fundamental enzyme, is 98 percent inhibited in Alzheimer's patients. They also discovered that tubulin — a major brain protein that holds an axon in its extended form and controls the growth direction of axons and dendrites — is inhibited by more than 80 percent.

In 1989, he published the paper2 "Aberrant guanosine triphosphate-beta-tubulin interaction in Alzheimer's disease" in the Annals of Neurology, stating that "These results support the hypothesis that microtubule formation is abnormal in brains affected by Alzheimer's disease."

Haley goes on to recount the story of how he got into trouble with the NIH when he decided to investigate the influence of heavy metals on Alzheimer's susceptibility. A popular theory at the time was that Alzheimer's was caused by aluminum toxicity.

Using his technology, he was able to show that mercury was the only heavy metal capable of causing a normal brain to develop the same biochemical abnormalities — including abnormal tubulin — that you find in Alzheimer's disease.Haley claims his research has since been replicated and confirmed. According to Haley, mercury causes the synaptic clefts to disappear and triggers the formation of neurofibrillary tangles, a major diagnostic hallmark of Alzheimer's, by causing abnormal hyperphosphorylation of tau.

He also published a paper3 in the respected medical journal Proceedings of the National Academy of Sciences in 1992, detailing how the presence of glutamine synthetase in the cerebrospinal fluid may be a potential diagnostic biochemical marker of Alzheimer's disease, as well as more than 100 other studies,4 including a review of the relationship between mercury and autism,5 and research showing how the chelating agent he developed, emeramide (NBMI), protects against the cytotoxicity of mercury.6


Do 10-06-2021 05:19:47
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