Amino acid of L-Glutamine

L-Glutamine, the most abundant amino acid in muscle tissue, is partly responsible for the transport of nitrogen into the cell for muscle growth and the extraction of ammonia way from muscle tissue. The ‘L’ indicates a natural form of the amino acid glutamine.

It is nonessential amino acid which is synthesized from branched chain amino acids (BCAAs) by transamination requiring the enzyme glutamine synthase.

L-Glutamine makes up approximately 50-60% of the free amino acid within cells but less than 10% of the structural protein within skeleton muscle.

L-Glutamine provides an important contribution muscle growth through protein synthesis an increased growth hormone levels in a recent study by the American Journal of Clinical Nutrition.

In American Journal of Clinical Nutrition 1995, scientists reported that a single 2-gram dose of L-Glutamine can elevated circulating growth hormone levels by over 430%.

Growth hormone is responsible for glucose and amino acid uptake within the body, muscle growth due to protein synthesis and the utilization of fat stores for energy.

L-Glutamine is present in large amounts in the lining of the digestive tract. When muscles or the lining of the intestinal tract are damaged, glutamine plays a vital role in the process that fixes the damage.

It can be exceptionally useful in cases of food poisoning or infection through is action to slow diarrhea. In general it slows down transit time by restoring mucosal function.

L-Glutamine   is metabolized to glutamate, aspartame, lactate and pyruvate and is a substrate for the production of glutathione which is important in antioxidant intracellular defense mechanisms.
Amino acid of L-Glutamine    

Synthesis of glycogen

The biosynthesis of glycogen in liver and muscle is linked to the nutritional status of the body, as represented directly by blood nutrient levels and individual directly by the concentration of hormones such as insulin, glucagon, catecholamines and glucocorticoids.

Stimulation of glycogen synthesis is one of the major physiological responses modulated by insulin.

The process occurs in the cytosol, and requires energy supplied by ATP and uridine triphosphate (UTP).

The synthesis of glycogen involves at least two distinguishable stages.

First by controlling the uptake and transport of glucose – the building block for the synthesis of glycogen molecule and secondly, by regulating the phosphorylation and activation states of enzymes involved in the synthesis and degradation of glycogen.

Most of the glycogen synthesis occurs through the lengthening of the polysaccharide chains of a preexisting glycogen molecule in which the reducing end of the glycogen is attached to the protein glycogenin. Glycogenin is a protein that attaches short chain of eight glucose molecules to the hydroxyl (-OH) group of a tyrosine residue on itself.

Glycogen synthase is responsible for making the α(1→4) linkages in glycogen.  This enzyme only elongates already existing chains of glucose.
Synthesis of glycogen

Synthesis of vitamin D from the sunlight

The major source of vitamin D for most land vertebrates, including humans, comes from exposure to sunlight.

Vitamin D in general refers to both vitamin D2 and vitamin D3, however vitamin D2 or ergocalciferol is the naturally occurring form in plants and vitamin D3 or cholecalciferol is the form synthesized by vertebrates.

During exposure to sunlight, the ultraviolet B photons enter the skin and photolyze 7-dehydrocholesterol (provitamin D3) to previtamin D3 which in turn is isomerizes by the body’s temperature to vitamin D3. 

Ultraviolet B that is penetrating through ozone layer is with energies 290-315 nm. As a result of the energy of this irradiation, the sterol ring structure is split to form previtamin D. This photolysis of 7-dehydrocholesterol to previtamin D3 occurs in the plasma membrane of skin cells.

No more than 15% of the initial provitamin D3 concentration ends up as previtamin D3.

Previtamin D3 then is ejected out of the plasma membrane into extracellular space where it enters the dermal capillary bed bound to the vitamin D binding protein.

Approximately , 50% of previtamin D3 is converted to vitamin D3 in 2 hours and as vitamin D3 is formed in the membrane, its’ open flexible structure is thought to escape into extracellular space.

Next previtamin D3 is converted to vitamin D3 or cholecalciferol, which then diffuses in to the blood and circulates to the liver.

In the liver, cholecalciferol are converted into calcidiol and then sent to kidneys. The kidneys perform the finale step – the formation of 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] which also called calcitriol. Calcitriol is the active form of vitamin D.
Synthesis of vitamin D from the sunlight

Amino Acids Function in Our Body

Amino Acids Function in Our Body
Glycine
Glycine is utilized by the liver to detoxify certain components of foods, such as benzoic acid. It may also be involved in the synthesis of several body components, such as bile acids. Glutamic acid may act as a source material for the synthesis of other amino acids.

Histidine
Histidine is needed for growth and for repair of human tissues and is converted to a substance that stimulates the secretion of hydrochloric acid in the stomach to facilitate gastric function.

Proline and hydrioxyproline
Proline and hydrioxyproline contain a structure found in hemoglobin (blood pigment) and in the cytochromes (compound essential for oxidation and reduction reactions in the body).

Arginine
Arginine is required for the detoxification of ammonia and amine resulting in the production of urea. It is often classified as nonessential because it can be synthesized from other amino acids in the body although, too often, in insufficient amounts.

Phenylalanine and tyrosine
Phenylalanine and tyrosine are used by the body to make the hormones adrenaline and thyroxine and are also involved in the formation of melanin, a pigment present in the skin, hair and part of the eye.

Tryptophan
Tryptophan is an amino acid from which a substance involved in the constriction of blood vessel is formed, and is present in components of blood involved in clotting.

Cystine, cysteine and methionine
Cystine, cysteine and methionine are source of a part of the structure of insulin and the keratin of hair and are involved with oxidation-reduction reactions in the body.

While protein eaten in excess of that required for growth or cellular repair may be utilized as a source of energy, it is not considered that they are efficiently utilized for this purpose.
Amino Acids Function in Our Body

Proteins

Proteins
Proteins are the chief organic constituents of muscles and other tissues. Proteins are the major components of the enzymes that regulate and carry out the general metabolism and functional process of living things.

Proteins are parts of the intracellular and intercellular structure of animals; they make up the structure and composition of many hormones and antibodies (disease related components)), and are concerned with many other factors to involved with body functions.

Proteins contain nitrogen, hydrogen, oxygen, and sometimes sulfur and phosphorus. All proteins contain nitrogen at a level of about 16%. The analysis of proteins is determined indirectly by analyzing for protein nitrogen, then multiplying the result by 6.25 to determine the actual amount of protein analyzed.

Because proteins contain carbon, they can be used as fuel since part of the molecule can be oxidized, sometimes involving deamination, to supply energy.

Proteins are required by humans for growth (protein synthesis) and for repair and maintenance of cells. Since mature adults have, in essence, ceased to grow, their protein requirement is less, per unit weight, than that of those who are still growing.
Proteins