PRODUCT IDENTIFICATION
TOXICITY
H.S. CODE
CLASSIFICATION
EXTRA NOTES
Endogenous antioxidant that plays a major role in reducing reactive oxygen species formed during cellular metabolism and the respiratory burst. Glutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer agents.
PHYSICAL AND CHEMICAL PROPERTIES
- 5.41 (octanol-water)
REFRACTIVE INDEX
NFPA RATINGS
AUTOIGNITION
FLASH POINT
EXTERNAL LINKS & GENERAL DESCRIPTION
Drug Information Portal (U.S. National Library of Medicine) - Glutathione
http://home.caregroup.org/
chemistry/function: L-Glutathione is a biologically active sulfur amino
acid tripeptide compound containing three amino acids L-Cysteine, L-Glutamic
Acid and Glycine. Most glutathione is found in the liver where it detoxifies
many harmful compounds to be excreted thru the bile. Some glutathione can also
be found in red and white blood cells, the lungs and the intestinal tract. The
primary biological function of glutathione is to act as a non-enzymatic reducing
agent to help keep cysteine thiol side chains in a reduced state on the surface
of proteins. Reduced glutathione is involved in the synthesis and repair of DNA,
helps to recycle vitamins C and E, blocks free radical damage and enhances the
antioxidant activity of vitamin C, facilitates the transport of amino acids, and
plays a critical role in the detoxification of harmful compounds. It is also the
base material for several other key antioxidant enzyme systems including
glutathione-peroxidase, glutathione-reductase, and glutathione-transferase.
Declines in glutathione concentrations in intracellular fluids correlate
directly with indicators of aging.
http://www.nutritionadvisor.com/
Glutathione
(L-gammaglutamyl-L-cysteinylglycine) is a tri-peptide of the amino
acids cysteine, glycine, and glutamic acid. Glutathione is an antioxidant
compound found in living animal and plant tissue. It takes up and
gives off hydrogen and is important in cellular respiration. A deficiency
of glutathione can cause hemolysis (destruction of red blood cells,
leading to anemia) and oxidative stress. Glutathione is essential
in intermediary metabolism as a donor of sulfhydryl groups which
are essential for the detoxification of acetaminophen. [PDR Medical
Dictionary. Spraycar. 1999] Selenium is a structural component of,
and a co-factor for the antioxidant enzyme glutathione peroxidase.
Glutathione is the major endogenous antioxidant produced by the
cell. Glutathione participates directly in the neutralization of
free radicals, reactive oxygen compounds, and maintains exogenous
antioxidants such as vitamins C and E in their reduced (active)
forms. In addition, through direct conjugation, glutathione plays
a role in the detoxification of many xenobiotics (foreign compounds)
both organic and inorganic. Glutathione is an essential component
of the human immune response. Proposed mechanisms of immune enhancement
include: optimizing macrophage functions, offsetting oxidative damage
associated with lymphocyte monoclonal expansion, and stabilizing
the mitochondrial membrane thereby, reducing apoptosis in lymphocytes
Local:
Peptide
is the members of the compounds composed of two or more amino acids joined by
the linking between one amino acid residue and the carboxyl group of the next amino acid
by hydrolysis into linear,
branched or cyclical structures. The link is an amide bond, and is sometimes referred to as a peptide bond.
Peptides are playing a promising role in the molecular biology
and in the creating medicines. Peptides are used in the study
of protein structure and
function, antibodies for the inhibition of cancer, for the study of protein structure and
function research. Peptides are also used as instrumental in mass spectrometry.
Biological activities of peptide are applicable
in the fields of nutrition, medicine, and
cosmetics.
- Dipeptide: a molecule consisting of two amino acids
- Tripeptide a molecule consisting of three amino acids
- Octapeptide: a molecule consisting of eight amino acids
- Oligopeptide: a polypeptide composed of approximately 2-12 amino acids length (or 3 to 40 component amino acids)
- Polypeptide: a single molecule composed of approximately 13 or more amino acids.
- Protein: a linear polypeptides that are normally synthesized on ribosomes.
APPEARANCE
white to off-white crystalline powder
ASSAY
98.0% ~ 101.0%
LOSS ON DRYING
0.5%
TOTAL ASH
0.3%
OPTICAL ROTATION
-15.5° ~ -17.5°
RELATED SUBSTANCES
Complies with EP
CHLORIDES
200ppm max
SULPHATES
300ppm max
AMMONIUM
200ppm max
IRON
10ppm. max
RESIDUE ON IGNITION
0.1% max
SULPHATED ASH
0.1% max
HEAVY METALS
10ppm
As
2ppm
Cd
1ppm
Pb
1ppm
Hg
0.5ppm
MIEROBIOLOGY
TOTAL PLATE COUNT
1000cfu/g max
TOTAL YEAST & MOLD
100cfu/g max
E. COLI
negative
SALMONELLA
negative
STAPHYLOCOCCUS
negative
PARTICLE SIZE
100 mesh