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“Non-Denatured” Proteins verses “Denatured” Proteins
Why one promotes health and the other does not

The Importance of “Non-Denatured” Proteins
Educational Medical Considerations for “Non-Denatured” Proteins
Protein Discussion
Amino Acids Discussion
Essential Amino Acids
Non-Essential Amino Acids


Cystine Histidine Isoleucine Leucine
Lysine Methionine Phenylalanine Threonine
Tryptophan Tyrosine Valine


Aminoacetic Acid Alanine Arginine Aspartic Acid
Carnitine Citrulline Cysteine GABA
Glutamic Acid Glutamine Glutathione Glycine
Hydroxyproline Ornithine Proline Serine

The Importance of “Non-Denatured” Proteins

The term “non-denatured” protein simply means the protein is still in its natural state, the molecular double bonds have not been altered by heat.

Natural uncooked protein, as found in nature, has all of its molecular double bonds intact and correct. This means the molecules that make up the amino acids of proteins have very specific shapes. Cooking changes those double bonds, thus altering the molecular make-up of the very basic structures of the amino acids. A classic example is cooking an egg. The egg white, straight from the chicken, is clear and runny. Cooking turns the egg whites, white in color and firm. The higher the temperatures, or the longer the cooking times, the harder the egg white becomes. The majority of my patients develop severe food allergy reactions to eggs; eggs that is which have been cooked. I have yet to find a patient develop an allergy to chicken eggs, when they consume only raw eggs in their breakfast smoothie.

Protein powders are a huge money market in the USA. However, altering the molecular structures of proteins, makes all of the amino acids contained with that protein source worthless for human biology, except that calories are still being consumed. Heat causes the double bonds to become flip-flopped (changes the shape of the natural amino acid structures). Any protein worth its weight was processed using the lowest form of heat that technology can offer. The quality of consuming a protein in its natural state, is similar to eating only fresh, raw and organic vegetables, instead of eating your vegetables from a processed can.

The term “non-denatured protein” is an oxymoron. Since nearly ALL protein powder available to the public in modern cultures was processed using heat, high enough to alter all those double bonds; all proteins created using heat have been denatured. Meaning that several, most, or all of the double bonds that make a specific amino acid what it is, have been altered. Why then, do manufactures use heat to make their protein powders? Huge profit margins! Speedy manufacturing makes larger profits.

So why are “non-denatured proteins” the only good source of amino acid nutrition? There are hundreds of reasons, too numerous to list, so I will only cover one at this time, one perhaps few people are even aware exists. One that is extremely important. The answer is “Glutathione.”

Glutathione is an antioxidant which the human body makes on its own. It is each cell’s natural principle detoxification agent and the major pathogen inhibitor. Glutathione DEFICIENCY has three major implications. (1) The body loses it natural ability to drive out toxins. (2) Exogenous microbes (bacteria, viruses, parasites etc, that are NOT natural to the human body), can grow out of control. (3) Deficiency has been found to be a common denominator in autoimmune diseases and degeneration of brain tissues.

In my annual continuing educational seminars for Naturopathic Doctors, we frequently discuss Glutathione and it many benefits. Glutathione is one of the Naturopathic Doctor’s therapies of choice when working with degeneration of brain tissues in diseases such as ADD and ADHD, Alzheimer’s, Autism, Dementia, and Parkinson’s disease.

Doctors have tried giving patients both glutathione supplements as well as glutathione injections. The only method that was found to substantially increase natural Glutathione levels was taking a “non-denatured protein” on a daily basis. Readily available proteins did not raise patient’s glutathione levels, only the “non-denatured proteins.”

Is it hard to obtain “non-denatured proteins?” Yes. Stopping a protein from becoming “denatured” requires a very slow process of using the lowest technology of heat known to science. This causes a financial problem for manufactures. There is only one method know to science at this time, that can process proteins at heat levels low enough to keep all double bonds intact. This process is called: “Refractance Window Dryer Technology” As of 2016, there are only 21 known Refractance Window Dryers in the United States. Only four of these 21 are used in the manufacture of proteins. Three are owned by the company who manufactures the Vegan Protein I recommend for patients who have Goat Milk allergies. The forth is owned by a family run business that makes non-denatured protein powders from their organically raised goats on their goat farm. They only have one unit because they are a family run business and these units are very large and extremely expensive!

I test all my Nutritional Blood and Hair Analysis patients for food allergies. If they do not have any allergies to goat milk, then they can use any of the Goat Milk Proteins from that particular family run goat farm, or a specific Vegan Protein I recommend. The Vegan Protein I recommend is derived from Yellow Peas. Yellow peas are very HYPO allergic to patients. These two protein sources are the only proteins I recommend to my patients for all the reasons stated in this report.

Educational Medical Considerations for “Non-Denatured” Proteins

I only recommend four proteins for my patients who are protein deficient:

  • Protein that is made from Goat’s Milk, using Refractance Dryer technology. Goats that are raised on their own farm, at the same location where the goat’s milk is turned into all natural goat whey protein. Their goats are pastured on organic grass that is free from any chemicals.
  • Protein that is made from Organic Yellow Peas, using Refractance Dryer technology. Organic yellow peas are both high in natural proteins, yet remain extremely non-allergy forming for my sensitive patients.
  • Protein made from Dairy Whey, using Ultra Low Heat technology. The dairy cows are pastured only on organic pastures.
  • Protein made from Dairy Whey and low allergy potential Rice , using Ultra Low Heat technology. This makes an easy to digest protein for my sensitive patients.

Educational Medical Considerations for Refractance Dryer Processed Protein:
Educational Suggestions:
1) Goat Whey Protein, “Professional Formulas”
“Professional Formulas” is only sold through doctors with a valid license to practice medicine. Call our clinic.
2) Yellow Pea Protein, “Response Formulas Vegan Protein.” “Response Formulas Vegan Protein” is only sold through doctors with a valid license to practice medicine. Call our clinic.

Educational Medical Considerations for Ultra Low Heat Processed Protein:
Click on “Visit our Online Store”
Click on “Metagenics”
Click on “Health Categories” (under picture)

Category: “Body Composition”
Educational Suggestions:
3) Perfect Protein
4) UltraBalance Protein
Bonus: Protein Fusion Bar (travel bar)

Category: “General Wellness”
Educational Suggestions:
Bonus: Ultra Energy Bar (travel bar)

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Protein Discussion

Proteins are any of a group of complex organic compounds containing carbon, hydrogen, nitrogen and sulfur. Proteins, the principle constituents of the protoplasm of all cells, are of high molecular weight and consist of alpha-amino acids joined by peptide linkages. Different amino acids are commonly found in proteins, each protein having a unique, genetically defined amino-acid sequence, which determines its specific shape and function. They serve as enzymes, structural elements, hormones, immunoglobulins, etc. and are involved in oxygen transport, muscle contraction, electron transport, and other activities.

The importance of adequate protein intake to proper immune function has been extensively studied. The most severe effects of “Protein-Calorie Malnutrition” (PCM) are on cell-mediated immunity, although all facets of immune function are ultimately affected. PCM is not, however, a single nutrient deficiency. It is normally associated with multiple nutrient deficiencies, and some immune dysfunctions attributed to PCM are most likely due to these other factors. Partial deficiencies of dietary vitamins produce a comparatively greater depression on immune functions than do partial protein deficiencies. Non-the less, adequate protein is essential for optimal immune function.

High protein diets are not recommended for individuals with kidney or liver disease. There are no other known side effects.

Most Desirable Sources of Proteins are: Meats and eggs, but are not the best source of protein because these foods are usually subjected to high heat when cooked. (High heat “denatures” proteins.) Beans are an excellent source of protein, but should be prepared using as little heat as possible so the amino acid bonds within the proteins are not denatured. Raw seeds, nuts and sprouts are excellent sources because these are hopefully eaten raw. Nut butters such as peanut butter, cashew butter and almond butter are good sources of proteins, if these foods were manufactured without using any heat, or ultra low heat only. Quinoa, an ancient grain (something like millet), is also a quality protein source, especially if sprouted so it is not subjected to the high heats of baking. (It is also gluten free.)

Less Desirable Sources of Proteins are: Processed soy, processed diary (however RAW dairy is great), and processed luncheon meats that contain nitrates or nitrites.

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Amino Acids Discussion

One of a class of organic compounds containing the amino (NH2) and the carboxyl (COOH) group, occurring naturally in plant and animal tissues and forming the chief constituents of protein; many of them are necessary for human and animal growth and nutrition and hence are called Essential Amino Acids. Amino Acids are the building blocks of protein.

Depending upon the source of dated reference material studied, some reports state “20” Amino Acids have been identified. More modern reference materials state “22” Amino Acids have been identified. In my personal research, identifying all possibilities available to me at this time, I have listed “28” Amino Acids / or Amino Acid Derivatives. Of my 28 listings, 22 have been identified as “Commonly Occurring” in Proteins.

In living things, Amino Acids serve as the primary unit of synthesis both of Tissue Proteins and other Non-Protein Nitrogenous Compounds.

Amino acids may undergo complex inner conversions in the body into macromolecules such as carbohydrates, nucleic acids, lipids, etc. Mineral co-factors also play an important role in that they interact with enzymes to assist with their catalytic activities. They are also capable of complexing with the individual free amino acids. For example, magnesium (MG2+) is important in the phosphorylation process or the transfer of high-energy phosphate groups into the body. Upon entering the body any free amino acids undergo complex inner-conversions into those substances necessary to maintain the metabolic pathways in the body. For example, Phenylalanine goes to Tyrosine and Arginine goes to Citrulline and Ornithine. (The Arginine pathway is a very important cycle.) Amino acid inner-conversions are not limited to other amino acids. Many free form amino acids play important roles as precursors for metabolic intermediaries. An example of this, Tyrosine’s and therefore Phenylalanine’s ability to give rise to two hormones Thyroxsine and Epinephrine. The Sulfur containing amino acids often precurse Taurine, which is an important bio-acid component. As W.C. Rose observed in 1938, “Perhaps undo emphasis was placed upon the quantity of protein ingestion and that scant consideration was given to possible difference in nutrient quality.”

Upon ingestion of foodstuff all nutrients and amino acids do not immediately diffuse into the surrounding tissue of the blood stream, but must first undergo a series of steps of biochemical reactions in the digestive tract. These reactions reduce the protein into its’ individual amino acids. Protein cleaving enzymes are activated in the digestive process, but in order for this cleavage to occur energy must be supplied on the part of the individuals metabolism to break the peptide bonds. The tissues then selectively absorb only those amino acids possessing the L configuration. “Methionine has been shown, however to be metabolically inter-changeable in both its’ L & D forms.” Rose and Wicksman 1955

By starting with a free amino acid mixture in which all amino acids are in their L conformation little digestion is necessary. The result is an energy saving and rapid absorption into the blood stream and surrounding tissues. “Amino acid supplementation of foods and feeds bring about many beneficial results. Of practical importance is the attainment of a better balance of protein and therefore a better balanced diet, an extension or savings of the available protein supply, and an improvement in the efficiency of the protein and food utilization. ” Rosenburg – 1959

Functional Identity of Amino Acids:

Of all the fundamental amino acids, 10 (ten) are classified as “ESSENTIAL” and are NOT biosynthesized by the body. All commonly occurring amino acids can be subdivided into 5 fundamental groups each of which has functional significance.

Group #1 – This group includes all the amino acids possessing aliphatic properties (those whose carbon atoms are joined in open chains), Glycine, Alanine, Leucine, Valine, Serine, Threonine, and Isoleucine.

Group #2 – These are the Sulfur containing amino acids, Methionine, Cystine, Cysteine.

Group #3 – These amino acids are the acidic amino acids, (those that can donate a hydrogen ion), Aspartic Acid, Glutamic Acid, and their associated amids.

Group #4 – These are the diamino acids (those with additional NH2 groups), Arginine and Lysine.

Group #5 – These are the cyclic and aromatic amino acids, Phenylalanine, Tyrosine, Tryptophan, Histidine, Proline, and Hydroxyproline that is synthesized from Prolamine.

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Essential Amino Acids

Estimated Minimum Requirements of Adults for Essential Amino Acids

Amino Acid Women/milligrams/day Men/illigrams/day
Cystine 55 1000
Isoleucine 450 700
Leucine 620 1100
Lysine 1200 1500
Methionine questionable 1100
Phenylalanine 0220 1010
Threonine 0310 0500
Tryptophan 0160 250
Tyrosine 900 questionable
Valine 650 800

Histidine: Is not listed as essential for adults, but is very essential for infants.
An amino acid obtainable from many proteins by the action of sulfuric acid and water; it is ESSENTIAL for optimal growth in INFANTS. Its decarboxylation results in formation of histamine.
1. Release of histamines from body stores are required for sexual arousal.
2. Reported useful in alleviating pain associated with rheumatoid arthritis.

(Should be taken with vitamin C; Should be used with caution with Manic Depressives with elevated histamines; Should be used with caution in woman with severe depression or suicidal tendencies due to Premenstrual Syndrome; Is considered a mild neurotransmitter)

Cystine: An essential, Sulfur-containing amino acid, produced by digestion or acid hydrolysis of proteins, sometimes found in the urine and kidneys, and readily reduced to two molecules of Cysteine.
1. Reported helpful in dermatological conditions.
2. Promotes faster recovery of tissue after surgery.
3. Part of the Insulin molecule.
4. Found high in hair (sulfur bonds).

(Use caution with those persons predisposed to stone formation in the liver or kidneys)

Isoleucine: An essential amino acid produced by hydrolysis of fibrin and other proteins; ESSESNTIAL for optimal INFANT growth and for nitrogen equilibrium in adults.
1. Needed along with other branch chain amino acids for all rebuilding of muscle tissue.
2. Role in the release of energy during muscular work. (Metabolizes along the same pathway as fat.)

Leucine: An essential amino acid, ESSENTIAL for optimal growth in INFANTS, and for nitrogen equilibrium in adults.
1. Metabolized along the same pathways as fat.
2. Precursors of cholesterol.
3. Involved in the role of energy release during any work of the muscles.

Lysine: An essential, naturally occurring amino acid, ESSESNTIAL for optimal growth in human INFANTS, and for maintenance of nitrogen equilibrium in adults.
1. Reported to inhibit growth and replication of herpes simplex and Epstein Barr viruses (EBV).
2. Promotes bone growth in infants.
3. Stimulates secretion of gastric juices.
4. Found in abundance in muscle tissue, connective tissue and collagen.
5. Low in vegetarian diets.

Methionine: An essential, naturally occurring amino acid, which is an essential component of the diet, furnishing both methyl groups and sulfur necessary for normal metabolism.
1. Prevents deposits and cohesion of fats in the liver.
2. Gives rise to Taurine (an important inhibitory neuro modulator in the brain).
3. Involved in synthesis of Choline (Must be given with Vitamin B6 (paradoxial-5-phosphate) to inhibit synthesis of homocysteine which promotes plaque deposition in the arteries.)

Autistic Patients: “Taurine is deficient in Autistic patients; Methionine has an altered abnormally normal to high level, with anything distal to the Methionine pathway being low. Since Taurine is so important in the intelligence quotients of most species, this seems to be a significant.” Alpha A – Leverton, Protein and Amino Acid Nutrition (1959) B – Rose, Journalism of Biological Chemistry 217:977, 1955. (Taurine is distal to the Methionine pathway.)

Phenylalanine: An essential, naturally occurring amino acid, ESSENTIAL for optimal growth in INFANTS, and for nitrogen equilibrium in human adults.
1. May be useful in appetite control by stimulating CCK (Chaleceptokinin Enzyme) secretion.
2. Shown to be useful in management of certain types of depression.
3. Increases blood pressure in hypotension.
4. Gives rise to Tyrosine
5. It is one of the amino acids in the dypeptide sweetener Aspartain. (Aspartic acid and Phenolalanine)

(Should not be used in those with hypertension or using MAO’s (Monoamineoxydases).

Threonine: An essential, naturally occurring amino acid, essential for human metabolism.
1. Rises to three times it’s normal value at pregnancy.
2. Acts as a lipotropic factor.
3. Recently found to increase brain Glycine content, greatly reducing ALS symptoms. (Amyotrophic Lateral Sclerosis or “Lue Gehrig’s Disease.”)

Tryptophan: An essential, naturally occurring amino acid, existing in proteins and essential for human metabolism.
1. Reported useful in the management of depression and schizophrenia.
2. Produces Serotonin, which induces sleep. Has a Serotonengenic effect.
3. Precursor of the vitamin Niacin.
4. Vasoconstrictor, which appears to aid in blood clotting mechanism, aids in elevating the threshold of pain.

(Should be taken with Vitamin B6 (paradoxial-5-phosphate) and in the presence of carbohydrates such as fruit or vegetable juice to maximize uptake in the brain.)

Tyrosine: An essential, naturally occurring amino acid present in most proteins. It is a product of Phenylalanine metabolism and a precursor of thyroid hormones, catecholamines, and melanin.
1. Along with Phenylalanine, it is a useful anti depressant due to increased production of Tacolamine. (Recommended to be taken with Vitamin B6 (paradoxial-5-phosphate).)
2. Reported to stabilize blood pressure by lowering energy in some cases and elevating it in others.
3. Involved in tissue pigmentation
4. Is important in the formation of thyroid hormone

(Should not be used when MAO’s are prescribed or when cancer melanoma is present)

Valine: An essential, naturally occurring amino acid, essential for human metabolism.
1. Needed for all muscle building.
2. Required in the precursors of cholesterol.

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Non-Essential Amino Acids

Aminoacetic Acid: A nonessential amino acid, derived from many proteins, used as a gastric antacid and dietary supplement, and in the treatment of various myopathies and peripheral vascular insufficiencies. A solution is used as an irrigation fluid. Its hydrochloride salt is use as a source of hydrochloric acid in the treatment of achlorhydria.

Alanine: A natural amino acid occurring in two forms, alpha-Alanine, and beta-Alanine.
1. Hypoglycemia (Prolongs the stabilization of blood glucose over long periods of time.)
2. Alanine may be used for the production of glucose in gluconeogenesis.

Arginine: An amino acid occurring in proteins; it is involved in the urea cycle, which converts ammonia to urea.
1. Induces growth hormone release from the pituitary gland.
2. Major component of seminal fluid. A lack can lead to ED (Erectile Dysfunction).
3. Helpful in burn treatment, elevated ammonia levels, and cirrhosis of the liver.
4. Stimulates immune response by enhancing the production of T-Cells.
5. Protective effect of toxicity of hydrocarbons and intravenous diuretics.

(Should be used with caution in schizophrenic cases.)

(Intake should be kept low in persons with Herpes simplex and Epstein Barr Virus (EBV). Mechanism of interaction is believed because of possible replications of the Herpes and EB viruses.)

Aspartic Acid: A nonessential, natural dibasic amino acid, involved in transamination reactions, the ornithine cycle, and the formation of carnosine, anserine, purines, and pyrimidines.
1. Has a protective function over the liver.
2. Helps in detoxification of ammonia.
3. Promotes mineral uptake in the intestinal tract.
4. It is part of the sweetener Aspartain that is a dypeptide of the amino acids; Aspartic Acid and Phenylalanine.

Carnitine: A betaine derivative involved in the transport of fatty acids into mitochondria, where they are metabolized.
1. Suggested as useful in mobilization of surface fats such as cellulite.
2. Helpful in treatment of fatigue and when muscle weakness is present. Useful in the oxidation of long chain fatty acids. A major source of energy for tissues.
3. Reported as useful in myocardial ischemia (low energy metabolism by the heart).
4. Useful in clearing triglycerides from the blood.
5. Useful in metabolic abnormalities.

Citrulline: An alpha-amino acid involved in urea production; formed from ornithine and is itself converted into Arginine in the urea cycle.
1. Produces the amino acids, Arginine and Ornithine.
2. Detoxifies nitrogen containing waste products such as ammonia (a cellular toxin) and is therefore part of ammonia detoxification (urea cycle).
3. Stimulates growth hormone production.

Cysteine: A sulfur-containing amino acid produced by enzymatic or acid hydrolysis of proteins, readily oxidized to Cystine, sometimes found in urine.
1. Assists tissues damaged by alcohol abuse, cigarette smoke and air pollution through the detoxification of Acetalaldahide.
2. Helps maintain skin flexibility and texture by slowing abnormal cross linking of collagen (connective tissue protein which holds the skin together).
3. Promotes red and white blood cell reproduction and tissue restoration in lung affecting diseases.
4. Useful in iron deficient anemia and promotion of iron absorption.
5. Helpful in prevention of peroxidized fats and free radicals.
6. Converts to Cystinine in the absence of vitamin C.
7. One of the amino acids found in tripeptide Glutathione and GTF.
8. Hair contains between 10 to 16% Cysteine.
9. Heavy metal chelator.

(Should be used with caution in diabetics due to possible three dimensional structure changes in the insulin cycle)

GABA – (Gamma Amino Butyric Acid): An amino acid that is one of the principle inhibitory neurotransmitters in the central nervous system.
1. Useful in schizophrenia and epilepsy, depression, high blood pressure, high stress levels, manic behavior, and acute agitation due to increased regulation of nerve firings and enhancement of Niacinamide binding receptors.
2. May induce calmness and tranquility by inhibiting neurotransmitters, which decrease the activity in neurons.
3. May be useful in reducing an enlarged prostate due to the suppression of Prolactia released by the pituitary gland.

Glutamic Acid: Glutamate is a salt of Glutamic Acid; in biochemistry, the term is often used interchangeably with Glutamic Acid. Glutamic Acid is a crystalline dibasic nonessential amino acid, widely distributed in proteins, which is thought to be a neurotransmitter, inhibiting neural excitation in the central nervous system; its hydrochloride salt is used as a gastric acidifier. The monosodium salt of L-Glutamic acid (sodium glutamate) is used in treating encephalopathies associated with hepatic diseases, and to enhance the flavor of foods and tobacco.
1. Reported useful in Muscular Dystrophy.
2. Does not cross blood brain barriers.
3. It is an excitatory neurotransmitter in the CNS; (Precursor of GABA.)

Glutamine: The monoamide of Glutamic Acid, an amino acid occurring in proteins; it is an important carrier of urinary ammonia and is broken down in the kidney by the enzyme glutaminase.
1. Is useful in treatment of Alcoholism by reducing the desire to drink.
2. May be helpful in the improvement of Autism and mental retardation in children.
3. Reported improvement in mental functions such as memory and dexterity.
4. Aids peptic ulcer healing due to antacid quality.
5. Crosses Blood brain barriers.
6. Participates in nucleonic acid synthesis
7. Converts to Glutanic acid.

Glutathione: Reduced Glutathione, a tripeptide of Glutamic Acid, Cysteine, and Glycine, which serves as a reducing agent in many biochemical reactions being converted to oxidized Glutathione (GSSG) in which the Cysteine residues of two Glutathione molecules are connected by a disulfide bridge. Reduced Glutathione is important in protecting erythrocytes (red blood cells) from oxidation and hemolysis; deficiency causes sensitivity to oxidant drugs.
1. It is a tripeptide containing amino acid that contains: Cysteine, Glycine, and Glutamate.
2. Inhibits peroxide formations, reducing free radical damage.
3. Detoxifies aromatic hydrocarbons common in air pollution, such as chlorine. Reported to have protective function against radiation therapy.
4. Transports other amino acids into the interior of the cell.

Glycine: A nonessential amino acid, occurring as a constituent of proteins and functioning as an inhibitory neurotransmitter in the central nervous system; used as a gastric antacid and dietary supplement, and in the treatment of various myopathies.
1. Is the simplest and sweetest of the amino acids. Can be used as a sweetener in herbal beverages.
2. Reported useful in degenerative diseases such as MD (Muscular Dystrophy)
3. Detoxifies benzoic acid (a common food additive) and aromatic hydrocarbons in the liver.
4. Involved in synthesis of nucleic acids and bio-acids. May be useful in conditions characterized by abnormal nerve firing such as epilepsy, inhibition of tripeptides Glutathione and GTF.
5. Is one of the amino acids in the tripeptides Glutathione and GTF; low brain concentrations of Glycine have recently been found in ALS. (Amyotrophic Lateral Sclerosis or “Lue Gehrig’s Disease.”)

Hydroxyproline: An amino acid produced in the digestion of hydrolytic decomposition of proteins, especially collagens.

Ornithine: An amino acid obtained from Arginine by the splitting of urea; it is an intermediate in urea biosynthesis.
1. May reduce fat and increase muscle mass by promoting fat metabolism and stimulating growth hormone production.
2. Helps in detoxification of ammonia in the urea cycle.
3. May be useful in autoimmune disease such as arthritis.

Proline: A cyclic amino acid occurring in proteins; it is a major constituent of collagen.
1. Is an anti-hypotensive agent in lowering high blood pressure.
2. Reported helpful in repairing muscle and tendon damage.
3. Reported useful in promoting skin flexibility in relation to aging and sun exposure.
4. A major amino acid found in collagen (connective tissue) in the presence of Vitamin C

Serine: A naturally occurring Amino Acid, present in many proteins.

Taurine: A crystallized acid, ethylamine sulfonic acid, from the bile; found also in small quantities in lung and muscle tissue.
1. Low levels seen in newborn infants fed low Taurine diets.
2. Associated with retinal degenerations.
3. The role of Taurine as a nutrient is to protect the cell membranes by attenuating such toxic compounds as oxidants, secondary bioacids and antibiotics.
4. Recommended for children on long-term parenteral nutrition.
5. Helpful in balancing calcium and potassium flux in heart muscle.
6. Helps patients suffering from congenitive heart failure by alleviating their physical signs and symptoms.
7. Increases left ventricular performance without any significant changes in atrial pressure.
8. Often times considered a neuro modulator.
9. Helpful in treating some types of epilepsy.
10. Does not readily pass across the blood brain barrier because of its two polar and non fat-soluble nature.

Autistic Patients: “Taurine is deficient in autistic patients; Methionine has an altered abnormally normal to high level, with anything distal to the Methionine pathway being low. Since Taurine is so important in the intelligence quotients of most species, this seems to be a significant.” Alpha A – Leverton, Protein and Amino Acid Nutrition (1959) B – Rose, Journalism of Biological Chemistry 217:977, 1955. (Taurine is distal to the Methionine pathway.)

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DISCLAIMER This information is provided for Educational Purposes Only and has NOT been designed to diagnose, treat or cure any health conditions. Please consult a qualified Health Care Professional with Nutritional Training to diagnose your health conditions and avoid self-diagnosis. The U.S. Food and Drug Administration have not evaluated statements about these health topics or any suggested product compositions.