Glycine
Scientific Name: Aminoethanoic acid (C2H5NO2).
Other Names: Gly, G, aminoethanoic acid.
Glycine is the simplest of the twenty standard amino acids and is nonpolar.
Because it has no side chain, it can fit into many other molecular structural locations that other amino acids cannot.
It is the most fundamental of all amino acids, and others are actually formed from glycine.
Origin: Glycine can be produced by the body in sufficient amounts to meet the needs of a typical human, making it a non-essential amino acid.
Free glycine is found in body fluids and in plants.
Sources of Glycine: As a supplement, glycine is available in several forms.
Capsules and tablets can be found, with a typical dosage of 500-600mg each.
Powder form is available for inclusion in protein shakes, and a .5 percent solution is available for injection purposes.
Home Remedies using Glycine:
Benefits and Uses of Glycine:
Glycine is an inhibitory neurotransmitter in the spinal cord, retina, and brain stem, as well as other parts of the central nervous system, meaning that it controls and prevents overstimulation.
Supplemental glycine has been shown to possibly have properties which have anti-spastic effects, as well as the ability to slow or stop psychotic activity.
It may also be of assistance as an anti-inflammatory and has antioxidant properties.
It has been used to treat diseases and disorders causing seizures and convulsions, and early studies are underway to determine its effectiveness in lipid metabolism.
Side Effects of Glycine:
Glycine is sometimes converted into ammonia and should not be used as a supplement by women who are nursing or pregnant.
In studies, frequent but mild gastrointestinal side effects of glycine supplementation were noted.
In humans, however, there are no known amounts for over dosage.
Additional Information for Glycine:
Aside from collagen, which is about one-third glycine, most proteins contain only a small quantity of glycine.
In proteins such as hemoglobin and myoglobin, the evolution of glycine into another amino acid is halted because mutations that change it into an amino acid with a larger side chain can actually disrupt the structure of the protein.
