Monday, March 21, 2011

Amino Acids. Do you know what they are?

One of our Jungle animals had this quarry: "What are Amino Acids". We hear a lot about them but it is always good to refresh our information.  So, get comfortable, for this is a long reading but definitively worth it. This is Jungle Miami's post today.

Understanding Amino Acids

(Autumn 2000 Optimum Nutrition Magazine)

Amino acid requirements are tremendously increased by disease, prolonged periods of stress and inborn metabolic errors. Billie J Sahley Ph.D, Executive Director of the Pain & Stress Centre in San Antonio, USA, and co-author of Healing With Amino Acids highlights some of the latest research on amino acids in therapy

Proteins control almost every biochemical reaction in the body. Every protein is made from amino acids, which are commonly called the building blocks of life. All of the nearly 40,000 distinct proteins found in the human body are made up from only 20 amino acids called the proteogenic amino acids.

Amino acids can be divided into essential and nonessential. Essential amino acids cannot be synthesised in the body and must be obtained from the diet. Non-essential can be synthesised in the body, and are not mandatory in the diet. Although the body can manufacture non-essential amino acids, an abnormality in their production can be detrimental metabolically. There are some conditionally essential amino acids which are essential under certain circumstances, i.e., infancy, illness, stress, etc.

Most of the protein in the body is found in the skeletal muscles. Only 0.1% of all the protein is found as free amino acids. Plasma amino acids represent what is available to the body at the current time. A deficiency in one of the proteogenic amino acids can limit the body’s ability to make an optimal number of certain proteins. Deficiency effects result in both poor health and disease.



The branched chain amino acids include leucine, isoleucine, and valine. As essential amino acids, BCAAs must be obtained from foods. They are especially involved in stress reactions, energy and muscle metabolism. BCAAs are unique because the skeletal muscles use them directly as an energy source, and they promote protein synthesis.

The BCAAs are similar structurally, but have different metabolic routes. Leucine solely goes to fats; valine solely to carbohydrates; and isoleucine to both. A valine deficiency appears as neurological defects in the brain. Muscle tremors mark an isoleucine deficiency. Stress states such as infections, trauma, surgery, fever, cirrhosis and starvation require proportionally more leucine than valine or isoleucine. Diseases such as hepatitis, cirrhosis, hepatic coma or liver disease, lower the levels of BCAAs. BCAAs, as well as other amino acids, are commonly fed intravenously to chronically ill patients. The BCAAs, particularly leucine, stimulate protein synthesis, increase the re-utilisation of other amino acids in many organs, and decrease protein breakdown.

As stress rises, total caloric intake needs increase, primarily due to increased protein requirements. Stress causes proteins to break down rapidly, and increases amino acid utilisation three-to-four-fold. About 30% of the diet should be protein or amino acids, especially when the body undergoes severe stress. But when taken in supplement form, BCAAs decrease the rate of amino acid and protein breakdown. More BCAAs and vitamin B6, or pyridoxal 5’phosphate (P5’P), are needed as stress or disease accelerates.

Utilisation of BCAAs by athletes, especially weight lifters, in-creases available energy. They help replace steroids used by those who want to build muscle mass. The BCAAs, especially leucine, greatly produce energy under many kinds of stress from trauma, surgery, fever, infection, muscle training, and weight lifting. With prolonged exercise, about 5 to 10% of the energy used comes from amino acids, especially BCAAs. Normal dosage of BCAAs is 1,000 to 3,000mg per day, divided. They should be taken together as the ingestion of only one BCAA, particularly leucine, decreases the plasma tissue levels of valine and isoleucine.


Alanine is a non-essential amino acid, and functions as an inhibitory neurotransmitter in the brain. Highest concentrations of alanine are found in the muscles. During hypoglycaemia, alanine may provide an alternative source of glucose.

Elevated alanine levels in the blood can cause drug-resistant seizure disorders or severe depression. Low alanine levels are often seen with low glycine and taurine, and when the BCAAs are deficient. Normal alanine metabolism requires the presence of vitamin B6. Alanine is essential for the normal metabolism of tryptophan.

Best food sources of alanine include wheatgerm, turkey, duck and cottage cheese. Usual supplemental dose range is 200 to 600mg, daily.

"Recent research indicates stored body fat into carnitine plays an important role in converting energising the heart, reducing angina attacks, energy, controlling hypoglycaemia, and is beneficial in the treatment of diabetes, liver and kidney disease."


Aspartic acid is a non-essential amino acid and a major excitatory neurotransmitter. Formed in the body from glutamic acid with the presence of vitamin B6, aspartic acid plays a major role in the metabolism of ammonia via the urea cycle. Aspartic acid also metabolises carbohydrates via the Krebs cycle, and forms constituents of DNA called pyrimidine and orotates. Research indicates aspartic acid may be a stimulator of the thymus gland and the immune system.

Elevated aspartic acid levels may be seen in some patients with depression, epilepsy, stroke, high BCAAs, and low ornithine. Asparagine forms from ATP and aspartic acid, and can convert back into aspartic acid, if needed by the body.

Good food sources of aspartic acid include meats such as pork, turkey, chicken and wild game, wheatgerm, cottage and ricotta cheeses.


Carnitine was discovered in 1905 from extracts of meats, but no physiological role for it could be found until 50 years later. Early research indicated carnitine to be essential to the diet, but later it was discovered the body produced carnitine from lysine and methionine, provided sufficient amounts of niacin, vitamin B6, C, and iron were present. If a carnitine deficiency exists, deficiencies of lysine and methionine also exist. Concentrations of carnitine are 40 times greater in the muscles than in the plasma. Major sources of carnitine in the diet are meat, especially organ meats such as liver; and dairy products. Vegetables, grains and fruit contain little or no carnitine.

In 1973 research showed carnitine deficiencies exist in some people for various reasons. Between 1980 and 1983, almost 300 studies were published investigating carnitine's nutritional value and anomalies of carnitine metabolism causing clinical symptoms. Some carnitine deficiency symptoms include impaired lipid (fat) metabolism; lipid accumulation in the skeletal muscles, heart muscle, and liver; and progressive muscle weakness with a build-up of fats in the muscle cells. In children, carnitine deficiency may manifest as loss of muscle tone, failure to thrive, swelling in the brain, recurrent infections, hypoglycaemia and heart disturbances.

Carnitine is essential for the transportation of long-chain fatty acids into the cells where fats can be converted to energy. Recent research indicates carnitine plays an important role in converting stored body fat into energy, energising the heart, reducing angina attacks, controlling hypoglycaemia, and is beneficial in the treatment of diabetes, liver and kidney disease. Carnitine primarily regulates fat burning in the body. It transports large fat molecules into the part of the cells where fats can be converted into energy. If your level of vitamin C is low, you can have an apparent deficiency of carnitine. If carnitine is absent or deficient, many fats cannot be burned. Fats build up within the cell and bloodstream as triglycerides and cholesterol. Carnitine supplementation significantly reduces serum triglycerides and cholesterol levels, while increasing HDL (high density lipoprotein or “good” cholesterol). Dosages are 1,000 to 3,000mg per day, divided.


Cysteine is considered conditionally essential, and is one of the sulphur-containing amino acids. Cystine is the stable form of cysteine. Conversion of one to the other occurs in the body, as either is needed. If vitamin C is not present, cysteine converts to cystine. Cysteine spares methionine (another important amino acid) and can completely replace dietary methionine if the diet is supplemented by appropriate amounts of folic acid and vitamin B12.

Cysteine resides abundantly in proteins such as keratin in hair (12%) and trypsinogen (10%). It also acts as a detoxifier. Heavy metals such as mercury, lead, and cadmium are “tied up” by cysteine so they can be removed from the body.

Cysteine may protect heavy drinkers and smokers against acetaldehyde poisoning from chronic alcohol intake or smoking, according to Dr Herbert Sprince at the V.A. Hospital in Coatesville, Pennsylvania, and Thomas Jefferson University in Philadelphia. Biochemist, Durk Pearson reports cysteine is effective “not only in preventing hangovers, but also in preventing brain and liver damage from alcohol, and in preventing damage such as emphysema and cancer caused by smoking.” Cysteine has been found to offer a degree of protection against radiation.

Amino Acids for Brain and Body Functions

A specialised form of cysteine known as N-Acetyl Cysteine (NAC), was first produced by Mead Johnson for the treatment of excess mucus. The primary use for NAC is as a mucus-reducing agent. Mucus strands are broken up to decrease viscosity and congestion associated with excess mucus and sinus drainage. Oral supplementation of NAC is used with allergies, bronchitis, chronic sinusitis, asthma, pneumonia, cystic fibrosis, and even the common cold. Supplemental NAC dosage is usually 600mg, two to three times daily. Diabetics should not use cysteine because it can cause glucose levels to change.


GABA (Gamma Amino Butyric Acid), an inhibitory neurotransmitter, is found throughout the central nervous system (CNS). GABA assumes an ever-enlarging role as a significant influence on pain, stress, anxiety, and depression as well as stress-induced illnesses. By January 1998, there were over 3,000 documents and texts on GABA, describing how it affects anxiety/stress in the brain.

If you examine a step-by-step process of what happens in the brain when you feel stress and anxiety, you would see how GABA works to slow down messages. Panic, anxiety, or stress-related messages begin to release numerous signals, and concurrently a physiological response begins to take place - the fight-or-flight syndrome.

Research done at The Pain & Stress Center, San Antonio, USA, in stress, with patients suffering from all types of pain, muscle spasms or anxiety/panic attacks, demonstrated pure GABA, 750 mg, can mimic the tranquilizing effects of Valiumor Librium without the addiction or fear of being sedated The unceasing alert signals from the limbic system eventually overwhelm the cortex (the decision-making part of the brain), and the ability of the cortex and the rest of the stress network becomes exhausted. The balance between the limbic system and, in fact, the rest of the brain to communicate in an orderly manner depends critically on inhibition. GABA inhibits the cells from firing, diminishing anxiety-related messages from reaching the cortex.

GABA fills certain receptor sites in the brain and body. This slows down and blocks the excitatory levels of the brain cells that are about to receive the anxiety-related, incoming message. When the message is received by the cortex, it does not overwhelm you with anxiety, panic or pain. You are able to maintain control and remain calm. But, if you are under prolonged stress or anxiety, your brain exhausts all the available GABA and other inhibitory neurotransmitters, thus allowing anxiety, fear, panic and pain to attack you from every direction. Your ability to reason diminishes.

Research done at The Pain & Stress Centre, in San Antonio, with patients suffering from all types of stress, pain, muscle spasms or anxiety/panic attacks, demonstrated pure GABA (750mg) can mimic the tranquilizing effects of Valium or Librium without the possibility of addiction or fear of being sedated. GABA fills the receptor sites in the brain and nourishes the brain with what should be there. The calming effect usually occurs within l0 to 12 minutes.


Glutamic acid is a non-essential amino acid which can be synthesised by the body, or be converted into glutamine and GABA. Glutamic acid is thought to be an excitatory neurotransmitter. It acts as a brain ammonia detoxifier.

Since glutamic acid can be manufactured from aspartic acid, ornithine, arginine, proline, and alpha-ketoglutarate, deficiencies of this amino acid have not been seen. Elevation of glutamic acid may be present in some schizophrenics, epileptics, and patients with gout. In fact, epileptics generally have an elevation of glutamic and aspartic acids, and have low levels of GABA, taurine, and glycine. Rich food sources of glutamic acid include ham, bacon, turkey, chicken, duck, cottage cheese, yoghurt, wheatgerm and muesli.


Glutamine is the third most abundant amino acid in the blood and brain. Glutamine, an inhibitory neurotransmitter, acts as a precursor for GABA, the anti-anxiety amino acid. It helps the brain dispose of waste ammonia, a protein breakdown by-product. Glutamine assists the body in muscle development when illness causes muscle wasting, sometimes seen following a high fever, chronic stress, or a traumatic accident. It also provides a major alternative fuel source for the brain with low blood sugar levels.

Glutamine's most important function is strengthening the immune system. It supports the multiplication of selected white blood cells which strengthen the body's defense system. Glutamine aids other immune cells in killing bacteria, healing wounds, and maintaining and supporting glutathione, as an important antioxidant. Glutamine also supports pancreatic growth.

Scientists at the National Institute of Health, USA, in 1970 found glutamine to be the most important nutrient for the intestinal tract. During times of illness, the body uses glutamine to help tissue repair in the kidneys, intestines, and liver. Leaky gut syndrome is recognised more often today due to the increased use of anti-inflammatory medications. This makes the intestines more permeable and allows substances and foods which do not normally pass into the circulation to cross. Food allergies can result, causing discomfort and pain. But glutamine helps the gut to heal and makes the intestines less permeable. Japanese researchers found glutamine helps stomach ulcers heal. It helps clear the body of waste through the kidneys and liver. For those with impending surgery, glutamine supplements should be considered before, during, and after surgery.


Glycine is a non-essential amino acid, and has the simplest structure of all the amino acids, resembling glucose (blood sugar) and glycogen (excess sugar converted in the liver for storage). As the third major inhibitory neurotransmitter in the brain, glycine readily passes the blood-brain barrier. The body needs glycine for the formation of DNA, collagen, phospholipids, and for the release of energy.

According to Ronald Kotulak in his book, Inside the Brain, glycine “helps trigger brain cells to fire electric charges and speed learning.” Glycine helps spasticity and seizures, and is involved in behaviours related to convulsions and retinal function. If taken orally, glycine increases the urinary excretion of uric acid, and is possibly a useful adjunct to gout. It is an essential intermediate in the metabolism of protein, peptides, and bile salts. Liver detoxification compounds, such as glutathione, must have glycine present for their formation.

Glycine removes heavy metals such as lead from the body, and also decreases the craving for sugar. It has been shown to calm aggression in both children and adults. When combined with GABA and glutamine, glycine influences brain function by slowing down anxiety-related messages from the limbic system. Glycine is also effective in alcohol withdrawal.

Being a very non-toxic amino acid, glycine can be used in both children and adults. It is found in high concentrations in meats and wheatgerm. Usual dosage range is 500 to 3,000mg, per day, in divided doses.


Histidine, one of the essential amino acids, is required in large amounts in infants. It is necessary for the maintenance of the myelin sheath of nerves and has vasodilating and mild anti-inflammatory properties. The neurotransmitter histamine derives from histidine. Histidine promotes large increases in brain histamine content, especially in the hypothalamus.

People with abnormally high amounts of histamine often demonstrate a history of psychiatric problems ranging from mild to severe. People with chronic pain and fibromyalgia demonstrate high histamine levels represented by joint swelling. High histidine and histamine levels are often seen in patients with obsessive-compulsive disorders, depression, and phobias. Low blood-histamine levels are found with rheumatoid arthritis and Parkinson's disease.

Best food sources of histidine include pork, wheatgerm, chicken, turkey, duck, ricotta and cottage cheese.


Lysine is an essential amino acid, and must be obtained from the diet, as it cannot be produced by the human body. Lysine is a critical protein required for growth, tissue repair; and production of hormones, enzymes, and antibodies. Additionally, it helps reduce the incidence of herpes outbreaks. The proper balance of lysine to arginine helps suppress the virus.

Symptoms of lysine deficiency include fatigue, inability to concentrate, irritability, bloodshot eyes, retarded growth, anaemia, hair loss, and reproductive problems.

Good food sources of lysine include eggs, meat, fish, milk, cheese and yeast. Amounts required for optimum health varies widely from person to person from 500 to 1,600mg per day, depending on their particular biochemistry. If outbreaks of herpes occur increase the amount to 3,000mg, daily, until the symptoms subside.


Methionine, an essential amino acid, represents one of the sulphur-containing amino acids. It is a methyl donor, critical for the formation of many important substances such as nucleic acids, epinephrine, choline, lecithin, carnitine, melatonin, collagen, serine, creatine, and deanol. Additionally, methionine can be a detoxifying agent assisting the removal of heavy metals such as lead from the body. Methionine is necessary for selenium to be absorbed and utilised. As an antioxidant, it helps protect the body from the effects of radiation. Normal metabolism of homocysteine requires vitamin B6 and methionine.

People with abnormally high amounts of histamine often demonstrate a history of psychiatric problemsExcess homocysteine can cause plaque formation in the arteries, leading to cardiovascular disease. If supplementing with methionine, always add vitamin B6 and folic acid to prevent a build-up of homocysteine. Methionine can be synthesised into cysteine, cystine, and taurine, if sulphur is present. Excess methionine has been suggested in one type of schizophrenia, while low levels are seen with depression. Supplementing with methionine helps lower histamine levels in the body, and sufferers of allergies, asthma, and chronic pain may find methionine supplementation helpful. Heroin addicts often have low pain thresholds and high histamine levels. Methionine helps lower the excess histamine levels usually present during heroin, amphetamine, or barbiturate withdrawal. In some depressed patients, methionine lifts depression with supplementation of one gram of methionine, morning and evening. Compared to MAO-inhibitor antidepressants, methionine proves more effective.

Good food sources of methionine include pork, sausage, duck, wild game, lentils, pumpkin, sesame and sunflower seeds, avocado, cottage cheese, cheese and wheatgerm.


Phenylalanine, an essential amino acid, functions as the parent substance, or precursor of tyrosine. Phenylalanine converts to tyrosine in the liver. Phenoketonurics (PKU) cannot convert phenylalanine into tyrosine because they lack the enzyme, phenylalanine hydroxylase.

Although phenylalanine is not found in the brain, it resides in many brain peptides, proteins, and neurotransmitters. Phenylalanine is the raw substance that produces several compounds of the catecholamine family responsible for the transmission of nerve impulses, assuming an adequate supply of phenylalanine. Norepinephrine, a major neurotransmitter, derives from tyrosine or phenylalanine. The amount of norepinephrine available to the brain is predisposed by the amount of phenylalanine or tyrosine available. Phenylalanine is one of the few amino acids readily converted into brain compounds like norepinephrine that control a person's mood. Phenylalanine or tyrosine helps give a positive, uplifting effect on mood, alertness, and ambition. Often, this amino acid is deficient in depressed people. Phenylalanine can also stimulate the release of cholecystokinin (CCK) that, in effect turns off the appetite.

Other phenylalanine derivatives such as epinephrine are excreted at the nerve terminals in the hypothalamus, and norepinephrine is excreted at the sympathetic nerve endings, giving rise to the fight-or-flight response. Norepinephrine is stored in presynaptic vesicles in certain central synapses. During times of stress, the body's adrenal glands are under immense pressure to produce epinephrine and norepinephrine. Often, they become low or depleted. This depletion can lead to depression and stress which can cause pain, anxiety, uncertainty and fear. Supplementing with phenylalanine or tyrosine helps to increase the level of norepinephrine in the brain. Many antidepressants work by increasing or manipulating the norepinephrine level in the brain. Often the drugs work by blocking the norepinephrine from re-entering the vesicles or pouches found at the synapse. The natural way to normalise brain levels of norepinephrine is with supplementation of tyrosine or phenylalanine. Therapeutic dosage ranges from 500 to 1,500mg per day. Phenylalanine should be used with extreme caution in hypertensive patients and should always be taken with food. People taking MAO inhibitors or tricyclic antidepressants should not use phenylalanine or tyrosine.

The DL-form of phenylalanine, or DLPA, has been found to be effective in the treatment of pain, and for depression resulting from pain. DLPA increases the production of PEA (phenylethylamine), norepinephrine, and endorphins. PEA is a neurotransmitter-type substance with a structural resemblance to amphetamine, a stimulant drug. Endorphins are the morphine-like neurotransmitters that decrease pain and gives a sense of well-being. DLPA increases endorphins by preventing their breakdown in the brain, so they remain there longer. If you use DLPA, the suggested amount is 750mg, four times daily.

Food sources of phenylalanine include dairy products such as cheese and milk, meats such as chicken, turkey, and duck; and pecans, sesame seeds, lima beans and lentils. Therapeutic dosages of DLPA range from 500 to 3,000mg per day, divided.


As a non-essential amino acid, proline is required for the formation of collagen; but vitamin C must be present. The body can manufacture proline from ornithine or glutamic acid and, if needed, convert it back into ornithine.

Elevation of proline may be found in alcoholics with cirrhosis, and in some patients with depression or seizure disorders. Convulsions, elevated blood calcium levels, and osteoporosis may be caused by excess proline from a genetic error.

Good food sources of proline include cottage and ricotta cheeses, eggs, pork, luncheon meats, wheatgerm, turkey and duck. Supplemental doses range from 500 to 1,000mg, with vitamin C.


Serine, a non-essential amino acid, is synthesised from glycine in the presence of folic acid and vitamin B6. It is involved in DNA synthesis and in combination with carbohydrates, may form glycoproteins. Serine is required for the formation of choline, ethanolamine, phospholipids and sarcosine, is necessary for the formation of neurotransmitters, and to stabilise cell membranes. Phospholipids are made from phosphatidylserine, and require the presence of methionine and folic acid. Excess serine may cause psychosis and elevation of blood pressure.

Good food sources include cottage and ricotta cheeses, wheat, wheatgerm, pork, luncheon meat, turkey, peanuts, and soya.


Taurine is now classified as a conditionally essential amino acid in the adult, but in infants and children, taurine is essential. Taurine is one of the sulphfur-containing amino acids, and in the adult is synthesised from cysteine and methionine, provided vitamin B6 and some zinc are present. Taurine is found throughout the body, abundantly in the heart muscle, olfactory bulb, central nervous system, and brain -hippocampus and pineal gland. Taurine participates in a multitude of functions in the body involving the gallbladder, brain, heart, eyes, and vascular system. In the heart, taurine is the most concentrated amino acid. It is involved in the heart muscle contractility and rhythm. After a heart attack the levels of taurine often decrease dramatically. Taurine seems to assist in cardiac heart function by acting as a diuretic and a heart stimulator with doses of two grams per day.

In the heart, taurine is the most concentrated amino acid. It is involved in the heart muscle contractility and rhythm. After a heart attack the levels of taurine often decrease dramatically Taurine proves effective in the treatment of epilepsy, acting as an anticonvulsant. Usual dosage of taurine for epilepsy is 3,000 mg per day, with a non-protein meal. A deficiency of taurine has been demonstrated in some patients with depression. A deficiency can add to chemical sensitivity and decrease the body's ability to detoxify chemicals. Taurine is necessary for the formation of one of the bile acids and for proper functioning of the gallbladder. The bile may be a route of excretion of chemicals detoxified by the body. Taurine is sometimes called upon to help control inflammation or infection.

When tryptophan intake is deficient, especially during periods of stress, serotonin levels drop, causing depression, anxiety, insecurity, hyperactivity, insomnia, and pain

Best food sources of taurine include meats and fish. The need for taurine increases whenever you experience more stress than usual or have an illness. Supplementation is necessary as the taurine need becomes greater than can be obtained from the diet. Usual dosage of taurine is 500 to 3,000mg per day, preferably on an empty stomach.


Threonine is an essential amino acid, and is the precursor to brain glycine. It is required for proper digestion and intestinal tract function. Threonine breaks down into glucose, and into the amino acids glycine and serine.

A deficiency of threonine suppresses the immune system. It has also been found helpful in multiple sclerosis cases and in some patients with agitated depression and mania. Good food sources include pork, turkey, wheatgerm, and cottage and ricotta cheeses.


Tryptophan is an essential amino acid, and must be obtained from the diet. It ultimately breaks down into serotonin, the calming neurotransmitter in the brain. Serotonin helps us feel calm, relaxed and in control.

Tryptophan is essential to maintaining the body's protein balance. When food that is protein deficient or lacking tryptophan is fed to growing or mature individuals, such foods fail to replace worn-out materials lost by the body during the organic activities of its cells, tissues, and organs. The amino acid tryptophan is exhausted by the vital activities of the body and, in turn, must be replaced to prevent atrophy of the body's structures.

One of the few substances capable of passing the blood-brain barrier, tryptophan plays a variety of important roles in mental activity. When tryptophan intake is deficient, especially during periods of stress, serotonin levels drop, causing depression, anxiety, insecurity, hyperactivity, insomnia, and pain. The body requires ample supplies of vitamin B6 for the formation of tryptophan. About 1% of ingested tryptophan is metabolised to serotonin. About 90% of tryptophan is metabolised through Knudsen acid to nicotinic acid.

Tryptophan is obtained in the diet every day. Many rich natural forms of tryptophan include: bananas, green leafy vegetables, red meat, turkey, dairy products, pineapple, avocados, eggs, soya, sesame and pumpkin seeds, and lentils. Large doses of tryptophan, when combined with niacinamide and vitamin B6, can enhance the conversion of tryptophan to serotonin.

When tryptophan intake is deficient, periods of stress, especially during depression, serotonin levels drop, causing anxiety, insecurity, hyperactivity, insomnia, and painCurrently, tryptophan is available only by prescription. It was removed from sale in 1989 because of a contaminated batch that caused EMS (esoinophiliamyalgia syndrome). The

U.S Food and Drug Administration (FDA) determined the cause was tryptophan and not the contaminated batch. It reclassified tryptophan as an unapproved experimental drug, and ordered recall of all products except where tryptophan occurred naturally. To date, tryptophan is still banned for sale in the US and UK.

But within the last couple of years, 5-HTP, or 5-hydroxytryptophan, has become available. Derived from griffonia seeds, a member of the legume family, 5-HTP is about 10 times stronger than tryptophan and is one step closer to serotonin. Suggested dosage is 50 to 300mg daily.

One study compared 5-HTP to Luvox, an antidepressant. Subjects with depression were given 100mg of 5-HTP, three times daily, or 150mg, of Luvox, three times daily. Evaluations were done at two, four, and six weeks. After two weeks, both groups reported a significant reduction in depression. By week four, 15 of 36 5-HTP patients and 18 of 33 Luvox patients reported at least a 50% improvement in depression symptoms. Final assessment demonstrated the 5-HTP patients had the greatest improvement and the least amount of treatment failures. Another study involving endogenous depression (arising from within the individual, in all likelihood genetic) demonstrated marked improvement in 69% of patients receiving 5-HTP.


Tyrosine is the first breakdown product of phenylalanine, and is considered a non-essential amino acid because the body can make it from phenylalanine. Dr Gelenberg, at Harvard Medical School, USA, determined tyrosine more effective than anti-depressants for relief of depression. The suggested amount of tyrosine is one 850mg capsule three times daily. Do not take tyrosine with MAO inhibitors or tricyclic antidepressants.


The body constantly conducts many complicated series of chemical reactions in precisely controlled ways to keep us healthy. Over 5,000 reactions occur every second in a cell. By utilising the natural substances in optimal quantities to re-establish a normal balance, you can help correct the cause of some disease processes in a non-toxic way.

Amino acid metabolism disorders are becoming recognised as a major factor in many disease processes. Amino acid testing is an analytical technique on the leading edge of nutritional biochemical medicine. It gives a new approach towards illness, and can assist patients who have not responded to treatment as expected, or who present complex cases with diverse symptoms.

Amino acid analysis of urine or plasma goes a long way towards assessing vitamin and mineral status. It measures the levels of amino acids in the body that affect many important processes. Additionally, it provides insights into the patient's functional needs for a wide variety of vitamins and minerals. Many of the enzymes which catalyse the interconversion of amino acids require vitamin and mineral co-factors to function optimally. In many cases where incomplete conversion of one product to another is due to sluggish enzymes, this indicates a functional need for increasing levels of a co-factor.

Amino acid analysis has proven helpful in treating:

•Chronic Fatigue

•Candida Infections

•Food & Chemical Sensitivities

•Immune System Disorders



•Learning Disorders

•A.D.D./ Hyperactivity

•Behavioural Disorders

•Eating Disorders




•Cardiovascular Disease




•Chronic Pain


Pyridoxal 5'Phosphate (Active B6)

Pyridoxal 5' Phosphate, or P5'P, the biological (active) form of vitamin B6 is necessary for the utilisation of all amino acids, proteins, fats, and carbohydrates. If P5'P is not present, increased excretion of most amino acids occurs as well as increased formation of abnormal amino acid metabolites. Unlike vitamin B6 there is no fear of toxicity with P5'P.


Magnesium is an essential co-factor in over 300 enzyme reactions in the body. Many individuals are deficient in magnesium, and do not get enough from their diets. Magnesium and vitamins B6, or P5’P must be present or the body cannot assimilate and use amino acids properly.


For most of the amino acids covered in this article, the therapeutic dosage and food sources are provided. Where the dosage is not stated, this indicates that the amount is variable, according to individual circumstances and needs. Where food sources are not stated, this indicates that the quantity of a particular amino acid from food sources alone is not high enough to produce a therapeutic effect.

In order to avoid biochemical imbalances, amino acid supplementation should be taken under the supervision of a nutritionist or health professional.

This article has been adapted from Healing with Amino Acids by Dr Billie J Sahley and Dr Katherine M Birkner (Pain and Stress Publications, 1998).

Billie J Sahley is Executive Director of the Pain & Stress Centre in San Antonio. She is a Board-Certified Medical Psychotherapist-Behaviour Therapist, and an Orthomolecular Therapist.

Katherine Birkner is a Pain Therapist at the Pain & Stress Centre. She is a Registered Nurse and Orthomolecular Therapist.

For further information regarding the therapeutic use of amino acids contact the Pain and Stress Centre, 5282 Medical Drive, Suite 160, San Antonio, TX 78229-602, USA. 001-800-669-2256

The Institute for Optimum Nutrition is an independent educational charity, registered charity number 1013084.

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For  IUPAC (International Union of Pure and Applied Chemistry) recommendations on AA (Amino Acids) and Peptide Nomenclature go to:


* From Jungle Miami: The information provided by this website is not intended as a substitute for medical advice.

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