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Amino Acids

In these cases, glutamine preparations are successfully used in many European clinics. Glutamine is usually prescribed in addition to the treatment of patients suffering from stress or injury (post-surgery, burns). Studies show that this use of glutamine helps reduce muscle loss in humans, since glutamine has a strong anti-catabolic effect.
Even in a normal state, the human body uses a huge amount of glutamine during the day. Especially a lot of glutamine is required to maintain the proper functioning of the immune system, kidneys, pancreas, gall bladder and liver. Glutamine also has the important function of transporting nitrogen, it removes ammonia from certain parts of the body (brain and lungs) and transports it to others (the kidneys and intestines). In addition, glutamine is used as a raw material for a strong natural antioxidant - glutathione (synthesized from glutamine, cysteine ​​and glycine).
In addition to all of the above, glutamine is among the few amino acids that cause additional production of growth hormone (somatotropic hormone, somatotropin).
Although this question already relates to the field of endocrinology, I will allow myself to briefly outline the peculiarities of the action of this hormone, since it plays an exceptional role in the metabolism.
The stimulating effect of growth hormone is not direct, but is associated with its effect on the formation of somatomedins in the liver. The main among somatomedins is somatomedin C, which in all cells of the body increases the rate of protein synthesis, which, in turn, leads to the stimulation of cell division and, as a result, the growth of muscle mass.
Factors affecting the secretion of growth hormone include starvation hypoglycemia, certain types of stress, and intense physical work. HGH is mainly released in a dream, the first release occurs after forty minutes, then every 2-3 hours while you sleep. Therefore, the first thing that can raise the level of growth hormone is a good rash. You can also stimulate the release of growth hormone by taking individual amino acids.
The most important substances that release growth hormone are also the amino acids ornithine, arginine, tryptophan, glycine and tyrosine, which act synergistically (that is, much more efficiently) with vitamins B6 and niacinamide, zinc, calcium, magnesium, potassium and vitamin C, “starting »Night release of growth hormone. Natural growth hormone levels decrease as they grow older. At the age of about 50 years, the production of growth hormone almost completely stops, but adding to the diet of amino acids and vitamins that stimulate its release, you can make the production of growth hormone the same as in youth.
Ornithine and arginine, two of several amino acids involved in the release of human growth hormone, are today one of the most popular amino acid supplements, mainly because they help you lose weight and improve your body shape while you sleep (that is, when the hormone is released growth). While some hormones encourage the body to accumulate fat, growth hormone acts as a fat mobilizer, helping not only to keep fit, but also to be more energetic. During the day, we draw energy from carbohydrates, and at night it is consumed from fat depots. In the daytime, when a person eats, the pancreas produces insulin, which helps burn carbohydrates and saves fats. And at night, the pituitary gland produces the so-called growth hormone, which ensures the burning of fat. Our body is very sparingly consumes fat reserves. After a late dinner, a lot of insulin is produced, which as it informs the pituitary gland that food has entered the body, and there is no need to spend precious fat reserves at night. As a result, the pituitary gland does not produce enough growth hormone. And the trouble is not only that at night we will not lose weight, as nature intended. Growth hormone has many other functions. Almost all cells of our body have receptors for it, and if growth hormone is not produced at night, all organs and systems suffer. And most importantly - with this, the body is rapidly getting old. After 35 years, the production of this hormone gradually decreases, and late dinner reduces it further, sharply accelerating the natural aging process. Ornithine stimulates insulin secretion and helps it show anabolic (muscle building) action, which is why the use of ornithine has increased among bodybuilders. Receiving an additional amount of ornithine helps to increase the level of arginine in the body (since arginine is formed from ornithine and ornithine from arginine as a result of their interconversion). Due to the fact that ornithine and arginine are so closely related, they have similar characteristics and should be taken with some precautions. In order for ornithine to fully manifest its properties, it must also be taken on an empty stomach, drinking water or juice, but not a liquid containing protein.
The strength exercises recommended from the middle of the second stage of the technique can raise the level of growth hormone, but they will be discussed later.
As for Glutamine itself, under normal nutritional conditions, a rather large supply of it is concentrated in the muscle tissues. Muscles are actually the storage sites for this amino acid and about 60% of the free amino acids contained in muscle cells are synthesized from glutamine.
If the intestines, the immune system and other organs cannot get enough of this amino acid from food, they begin to “plunder” glutamine reserves from muscle tissue, and a state of catabolism or muscle protein breakdown develops.
Since my goal is to protect patients from this condition, taking glutamine seems to be a worthwhile addition to any restrictions on protein intake from food.
Some doctors prescribe glutamine in large quantities, hoping at the same time, apparently, that he somehow gets to skeletal muscles. However, studies show that from 50 to 85% of a large oral dose of glutamine simply do not enter the bloodstream, breaking down under the action of gastrointestinal enzymes. And although there is no evidence of an overdose of glutamine, I am still convinced that a sharp increase in the content of any single amino acid in the serum is extremely undesirable. This can lead to its rapid deamination and, as a result, poisoning of the body.
I think it’s quite enough to give two or three grams of the glutamine drug twice a day. Moreover, only these two grams of glutamine, taken orally, lead, in fact, to a fourfold increase in the level of growth hormone (somatotropin) and immediately stop the catabolism of muscle tissue.
However, to normalize the state of muscle tissues that have already undergone partial destruction as a result of prolonged protein starvation, I would recommend taking four equal doses of glutamine per day for a while. Moreover, it is necessary that one of these doses accounted for at the end of physical activity, and the other was taken at bedtime.
Researcher Anthony Almada writes in his work that at a certain time (immediately after aerobic exercise or just before going to bed) we can meet the body's need for large amounts of glutamine by precise minimum dosage to preserve muscle structure and prevent their destruction.
Separately, it is worth emphasizing once again that when calculating the effect of a certain amino acid, its interaction with other amino acids in blood serum is of great importance. For example, glycine in combination with glutamine greatly enhances its effect, and alanine can maintain the level of glutamine in muscles, turning into blood into glucose. This is especially important in terms of limiting the number of calories consumed, when prescribing a "strict" diet or increasing the intervals between meals. Arginine has a high detoxifying effect and, with an excess of amino acids in the blood, is involved in the conversion of ammonium salts to urea.
Ornithine:
• reduces the amount of fat in the body;
• participates in the metabolism of muscle tissue;
• strengthens the immune system;
• contributes to the functioning and regeneration of liver tissue;
• participates in the formation of urea, ammonia detoxification;
• reduces the tendency to the deposition of fat in the body;
• promotes recovery from muscle fatigue;
• promotes energy exchange in the muscles.
Proline:
• the most important protein building material of the human cell.
Tyrosine:
• participates in the formation of norepinephrine, depressing appetite;
• stimulates the release of growth hormone, which in the presence of vitamin B6 increases muscle mass and reduces the level of fat in the body.
Phenylalanine:
• depresses appetite;
• stimulates the thyroid gland to produce thyroid hormones.
Histidine:
• participates in protein synthesis;
• is the precursor of glutamine.
Taurine:
• promotes the use of fats in the energy cycle.
In addition, amino acids include vitamin-like substances - Carnitine and Para-aminobenzoic acid.
L-carnitine (vitamin Bt).
Here are its main functional and biological characteristics:
• the process of its synthesis is activated in the presence of vitamins C, B6 and iron in the diet;
• it contributes to the oxidation of fatty acids in the mitochondria;
• transports long-chain fatty acids to mitochondria;
• regulates the concentration of ammonia in the blood;
• its beneficial effects occur when taken before exercise;
• increases maximum aerobic power and has a gentle glycogen effect;
• has an antiketogenic effect on a low-calorie diet;
• helps to get rid of excess subcutaneous fat;
It should be emphasized that the main point in the assimilation of any amino acids is elevated sugar and insulin in the blood. Insulin stimulates protein synthesis, which is manifested by a decrease in the blood level of amino acids having side chains (isoleucine, valine), due to their transport through the cell membrane into muscle tissue. Insulin has been found to increase the accumulation of 8 of the 20 naturally occurring amino acids in muscles. Insulin is the main anabolic hormone in the human body, which is responsible for the transport of amino acids into muscle cells and the further construction of these proteins from them. Although some recent discoveries in the field of biochemistry cast doubt on this priority role of insulin. The question remains how best to combine high levels of insulin with the intake of amino acids.
It seems to me that care should be taken to ensure that the diet in terms of supplements contains the necessary number of Q-factors. Perhaps the most important of these is chromium, in its optimal form for mastering - “chromium picolinate”. Chromium increases insulin sensitivity, and since insulin transports amino acids to muscles, it is quite obvious that the patient will be less able to absorb amino acids, lacking chromium.
Other important Q factors include zinc, which is a regulator of insulin, vitamins B6 and B12, which are important for protein metabolism, and biotin. A significant proportion of these Q-factors will come from a rationally compiled diet. But I consider it necessary to additionally assign correctly selected formulas of multivitamins with mineral complexes, the composition of which should be changed depending on the needs of the organism at different stages of the procedure.
In conclusion of the topic of proteins, I would like to express confidence that the biochemical laboratory, which has the technical ability to determine the amino acid composition of blood serum, in the near future will be included in the arsenal of each clinic that implements a modern approach not only to the problem of treating obesity, but also to other practical issues dietology. In this case, the consultant in biochemistry will become an indispensable employee of any clinical nutrition clinic.
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Amino Acids

  1. AMINO ACIDS
    A legitimate question may arise: what is secretin? Is its nature known, or is it just a name given to an unknown substance? The answer is: the nature of this substance is known, although not in every detail. Secretin is a protein, and proteins consist of large molecules, each of which contains hundreds, thousands, and sometimes millions of atoms. Compare this to a water molecule (H2O), which consists of three
  2. Amino Acid Absorption
    Digestion of proteins in the stomach occurs when pepsinogen is converted into pepsin in the acidic medium (optimum pH 1-3). Pepsin cleaves bonds between aromatic amino acids adjacent to carboxyl amino acids. Pepsin is inactivated in an alkaline environment. This stage of protein digestion is absent in patients after gastrectomy, as well as in those who have been taking inhibitors for a long time.
  3. CONGENITAL DISORDERS OF AMINO ACIDS
    Leon E. Rosenberg (Leon E. Rosenberg) All polypeptides and proteins are polymers of 20 different amino acids. Eight of them, called indispensable, are not synthesized in the human body, so they must be administered with food. The rest are formed endogenously. Despite the fact that most of the amino acids found in the body are bound in proteins, it’s still inside the cell
  4. Violations of the transmembrane transport of amino acids
    With effective intracavitary digestion in adults, only amino acids are absorbed (above 98%) using transmembrane transporters of amino acids (permease systems). In newborns and children 2-3 months of life, especially premature, with artificial feeding, absorption of short peptides, including antigenic ones, is possible with the formation of enteral cross
  5. FROM AMINO ACIDS TO KVERCETIN
    In the first publication, we talked in some detail about oncologist Wolfe Laskin, and therefore for those to whom she didn’t get into the hands, we will briefly describe how a practicing doctor, head of one of Moscow oncologic dispensaries, came up with the idea of ​​creating a therapeutic diet for cancer patients. Laskin was looking for a plant product rich in amino acids. Recall that by that time
  6. Diseases of amino acid metabolism
    Phenylketonuria Hereditary diseases in which the transport of amino acids through the intestinal mucosa and kidney tubules of the kidneys or their catabolism due to a deficiency of enzymes or coenzymes is disturbed General diagnostic criteria for metabolic disorders of amino acids require additional laboratory examination: 1) a combination of mental retardation with pathology of vision (homocystinuria, insufficiency
  7. Slowing up of amino acids in organs and tissues
    The amino acids absorbed from the intestines enter directly into the bloodstream and partially into the lymphatic system, representing the “metabolic pool” of various nitrogenous substances, which then participate in all types of metabolism. Normally, amino acids absorbed into the blood from the intestines circulate in the blood, are quickly absorbed by the liver and partly by other organs (kidneys, heart, muscles).
  8. Hereditary disorders of amino acid metabolism (aminoacidopathy)
    The relevance of considering interstitial amino acid metabolism disorders is determined by the fact that this pathology is reflected, first of all, on the function of the nervous system and is one of the main causes of dementia. Knowledge of this pathology is necessary in the practice of neonatologists and genetic laboratories for the prevention and early correction of oligophrenia. Phenylpyruvic oligophrenia (synonym -
  9. Pathology of interstitial protein metabolism (disturbance of amino acid metabolism)
    The main ways of interstitial protein metabolism are reactions of transamination, deamination, amidation, decarboxylation, peremetilirovaniya, re-sulfurization. The central place in the interstitial protein metabolism is occupied by the transamination reaction as the main source of the formation of new amino acids. Violation of transamination may occur as a result of deficiency in the body of vitamin Wb.
  10. Interruption of protein metabolism
    The pathology of this stage of protein metabolism is manifested by a violation of the interstitial (intermediary) metabolism of amino acids. Normal concentration of free amino acids in plasma is 4-8 mg / l. Acceptance of amino acids with food or their intravenous administration have little effect on this indicator. The main organs that utilize amino acids are the liver and kidneys. The brain absorbs amino acids selectively, preferring
  11. Genetic code. Properties of the genetic code
    The genetic code is a unified system for recording hereditary information in nucleic acid molecules as a sequence of nucleotides. The genetic code is based on the use of an alphabet consisting of only four letters A, T, C, and G, corresponding to DNA nucleotides. Since proteins contain 20 different amino acids, each cannot be encoded by one or two nucleotides (will be
  12. The value of protein in human life
    Properties of a protein depend on its composition and on the location of amino acids in the molecule. Moreover, the order of amino acids in the protein molecule plays a very important role in the performance of their functions. Amino acids synthesized in our body, called interchangeable. Some amino acids in the human body are not formed - it is an essential amino acid. Proteins containing the entire set of essential amino acids,
  13. Violations of the qualitative composition of proteins from food
    Of the more than 80 naturally occurring amino acids, only 22 are found in food proteins. Of these, 12 can be synthesized in the body, 10 are indispensable - arginine, valine, histidine, isoleucine, leucine, lysine, methionine, threonine, tryptophan, phenylalanine. The deficiency of any of them slows down growth, causes a negative nitrogenous balance associated with an increased breakdown of tissue proteins to extract the deficient
  14. PROTEIN EXCHANGE
    It is known that protein consists of amino acids. In turn, amino acids are not only the source. synthesis of new structural proteins, enzymes, hormonal, protein, peptide substances and others, but also a source of energy. Characterization of proteins that make up food, depends on both the energy value and the spectrum of amino acids. The average decay period of the protein varies in
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