NADH was discovered in 1905 and was found to be an essential co-factor or co-partner for all enzymes in the body, and therefore is commonly known as "coenzyme 1." Since its discovery, more than one thousand different physiological functions of NADH have been detected and extensively described in all biochemistry textbooks. We first learn about NADH at high school in biology of how the body makes energy from the food which we eat . However, NADH was viewed as so unstable—it could react to even small amounts of exposure to heat, light, or humidity—that it could not be used therapeutically. This was the reason that NADH has not been widely discussed before.
Fortunately, in the mid-1980s, researchers used modern-day technology to develop a stable, ingestible, and absorbable oral form of NADH that can improve the level of NADH in the billions of cells that make up the human body. A safe and effective form of NADH can now be used therapeutically.
NADH was used by Dr Walther Birkmayer for the treatment of Parkisons Disease.
NADH is biologically ranked and identified as coenzyme 1, the coenzyme or cofactor needed for numerous enzymes that are involved in the cellular energy production. A deficiency of NADH will result in an energy deficit at the cellular level, which causes symptoms of fatigue. When the body is deficient in NADH, it is kind of like a car that has run out of gasoline. The more NADH a cell has available, the more energy it can produce. Unfortunately, the production of NADH in our bodies declines as we age, and so does the production of NADH-dependent enzymes, particularly those enzymes involved in energy production.![]
NADH is present in all living cells of humans, animals, and plants. Hence, it is present in our daily food sources. However, animal protein sources—meat, poultry, and fish—contain the highest amount of NADH. Vegetables, fruits, and other vegetarian food have a much lower NADH content. Plants need less energy to survive and no energy for locomotion or movement, so they have less NADH. Vegetarians, therefore, receive little NADH from their diets and should consider supplementing with NADH.
Many other people also can benefit from taking NADH supplements, though, for a few key reasons. First, almost all of the NADH we take in from food is destroyed during food preparation. Second, even if our diets consisted mostly of raw meat or fish (which isn't advisable), we would only receive a minimum of NADH from these food sources. Most of the NADH in these foods would be degraded by the stomach's own digestive gastric acids that break down food into its constituent parts for absorption.
The NADH story began in a roundabout way in the late 1940s and 1950s. At that time, my father, Walther Birkmayer, MD, began exploring biochemical transmitter mechanisms within the human brain. His research led to the realization that injuries to the brain actually create an imbalance between various reactor substances or neurotransmitters, resulting in a wide range of patient behaviors and symptoms.
During the 1960s, my father discovered that L-Dopa (the synthesized form of the neurotransmitter dopamine) could relieve symptoms in patients with Parkinson's disease and allow these patients to experience increased mobility with less rigidity. The L-Dopa treatment, known under the brand name Sinemet, is now the preferred drug therapy for Parkinson's disease. However, L-Dopa treatment has one big drawback: It is given in very high amounts, causing an "overloading" of the body and the brain. This leads to a dangerous side effect: the production of enormous amounts of free radicals. Free radicals are highly active molecules that react with every substance in a cell and can damage cell membranes. Medical researchers also know that L-Dopa therapy becomes less and less effective over time, with more and more resulting side effects. This damage has been observed in patients with Parkinson's disease, particularly after long-term treatment.
The drawbacks to L-Dopa treatment prompted my father and me to develop a completely new treatment approach using NADH. We began using NADH in pure form for intravenous infusion in 1985. NADH worked because it naturally stimulates the body to produce its own dopamine. NADH was so unstable, though, that it needed to be given intravenously at a clinic or hospital, so this made treatment inconvenient and time-consuming. To make NADH easier to use therapeutically for our patients and others, we sought out and eventually developed a stabilized, absorbable, form of NADH that could be taken by mouth in easy-to-swallow tablets.