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Every food today is saturated with toxic substances that alter the alkaline pH and generate acidosis in the body. The cleaning process using ionized water in foot bath (such as Quick Cell Detox – in Italy DETOX DEEP) by rebalancing the basic acid indirectly neutralizes the acid in the blood, increases the metabolism and helps the body to adequately absorb the most effective nutrients to keep the body in wellness and slow down the aging process.
Ogni cibo oggi è saturo di sostanze tossiche che alterano il ph alcalino e generano acidosi nel corpo. Il processo di pulizia con utilizzo di acque ionizzate per immersione dei piedi (Quick Cell Detox -in Italia DETOX PROFONDO) attraverso il riequilibrio acido basico indirettamente neutralizza l’acido nel sangue, aumenta il metabolismo e aiuta il corpo ad assorbire in modo adeguato i nutrienti più efficaci per mantenere il corpo nel benessere e rallentare il processo di invecchiamento.

Former Secretary of Health Dr. Jaime Galvez Tan is Waters Philippines’ Wellness Ambassador
L’ex segretario della Salute Dr. Jaime Galvez Tan, Ambasciatore delle Acque Filippine è un medico multi-premiato  noto per la sua competenza medico-scientifica, per il suo importante lavoro nell’ambiente e per il suo approccio olistico alla guarigione

Quick Cell Detox usa una macchina che agisce per immersione dei piedi per una disintossicazione svolta in profondità. La macchina è stata realizzata ispirandosi ai due premi Nobel premiati per le due importanti scoperte: l’esistenza di canali d’acqua e i canali ionici nella membrana delle cellule.

The Nobel Prize in Chemistry 2003 was awarded “for discoveries concerning channels in cell membranes” jointly with one half to Peter Agre “for the discovery of water channels” and with one half to Roderick MacKinnon “for structural and mechanistic studies of ion channels”.

Two Americans Win Nobel for Chemistry

By KENNETH CHANG
Published: October 9, 2003

Two Americans won the Nobel Prize in Chemistry yesterday for work describing how water and charged atoms flow into and out of living cells through tiny pores.

The knowledge could lead to better understanding and potential treatments for diseases like cystic fibrosis, epilepsy and heart arrhythmia that arise when these gateways to the cell go awry.
Dr. Roderick MacKinnon, 47, a professor of molecular neurobiology and biophysics at Rockefeller University in New York City, was honored as the first to deduce the three-dimensional shape of one of these pores. Dr. Peter C. Agre, 54, a professor of biological chemistry and medicine at the Johns Hopkins University School of Medicine in Baltimore, won for the discovery of the first cellular pore known to convey water molecules.

The pores, or channels, are essential for the normal functioning of cells. The flow of charged atoms, or ions, generates electrical pulses that neurons and other cells use to communicate with one another. Scientists have long known that the channels are folded-up proteins piercing cell walls. Not only are these channels very specific about what they let through — just sodium ions or potassium ions, for example — but they can also be opened and closed like valves. By the 1980’s, scientists even knew the sequence of amino acids in many of these channel proteins, but they did not know the shape of the proteins, so they could not fully explain how the channels work — how a sodium channel keeps potassium ions out, or vice versa. Dr. MacKinnon’s drive to understand potassium channels led to a foray into a field of physics he knew little about. Trained as a doctor, Dr. MacKinnon studied the potassium through standard genetic techniques, creating a mutation in the protein and seeing whether it still functioned properly. While at Harvard University, he found a short sequence of five amino acids in the potassium channel that acted as a filter against sodium ions. If one of those was changed, then sodium would start flowing through the channel with the potassium. “Without seeing it, we wouldn’t know how it was doing it,” Dr. MacKinnon said. “We could tell what part of the protein was important, but we couldn’t tell why.” When he moved to Rockefeller in 1996, he began teaching himself a technique that determines the structure of protein crystals by bouncing X-rays off of them. Only one member of his research group at Harvard joined him at Rockefeller. “Most people thought this was too far out in the future, to actually determine a structure,” Dr. MacKinnon said. His wife, Alice, a chemist, joined him in his laboratory. “She started working with me, because she felt bad for me,” Dr. MacKinnon said. Within a couple of years, Dr. MacKinnon coaxed the potassium channel proteins into forming crystals and produced a three-dimensional picture of the channel.

And he found his answer: atoms in the channel surround a potassium ion in the same way that water molecules do, allowing the ions to effortlessly move into the channel. Sodium, smaller than potassium, does not fit as well and cannot pass through. “It was the first glimpse anyone had of a potassium channel,” said Dr. Steve A. N. Goldstein, a professor of pediatrics and cellular and molecular physiology at the Yale School of Medicine. “It showed that the hypotheses for how ion channels work were absolutely correct. More than that, it began to open a window to show the details we had not yet begun to appreciate. We could begin to look at them in more detail.” By contrast, Dr. Agre made his discovery by serendipity. In the 1980’s he was studying a particular protein found in blood when he found another protein contaminating his sample. “It really fell into our laps,” he said. “Being lucky is an important ingredient in scientific success.” When Dr. Agre and his colleagues tried to develop an antibody that would hook onto the protein they were studying, the antibody hooked onto the contaminant protein instead, so they decided to find out what types of cells contained the protein. It turned out to be one of the most abundant proteins found in blood cells — even though no one had seen it before. They looked for other similar proteins and found some in the roots of plants. No one knew the function of those proteins, either.  “It’s, like, curiouser and curiouser,” Dr. Agre said.

Finally, at the suggestion of a colleague, Dr. Agre tested whether the protein could be a water channel. Although some biologists suggested as far back as the mid-19th century that water channels might exist, most were dubious because none had ever been found. Instead, they believed that water moved through cell walls by diffusion, slowly pushing through.  To test the water channel hypothesis, Dr. Agre added the gene that produced the mystery protein to frog eggs. The modified eggs, placed in fresh water, quickly swelled and burst, indicating plenty of water flowing through the channels. “The things explode like popcorn,” Dr. Agre said.  The water channel proteins have since been found in other cells like those in kidneys, which extract most of the water out of urine and recycle it back into the body. Dr. Agre named the proteins aquaporins, or “water pores.”  In 2000, collaborating with other scientists, Dr. Agre produced a three-dimensional picture of the aquaporin. The channel is only a little wider than a water molecule.  Dr. Agre said that when his wife called his mother with the news that he had won the Nobel Prize, his mother said, “Oh, that’s very good, but don’t let it go to his head.”