Glutathione is the body’s master antioxidant and protects the body from various diseases. It performs multiple functions to prevent the body from developing diseases and also helps to detoxify chemicals and drugs.

On the other hand, its reducing level increases the risks of toxicity and diseases. GSH along with the other cellular antioxidants, work synergistically to neutralize and scavenge oxygen and other free radical species. Thereby it prevents or diminishes “oxidative stress”.

Progression of liver diseases is contributed by deficiency of GSH and increase of free radical species. Therefore, glutathione has an important role to play in the cases of alcoholic liver disease, viral hepatitis, and particularly hepatitis C.

Various studies were conducted related to the role of antioxidants, particularly L-glutathione, in chronic liver diseases. There were reports on the levels of glutathione present in liver, blood and lymphocytes of patients with chronic hepatitis C. Few of these patients were infected by HIV too.

The liver is the major source of GSH levels in blood. It was found that GSH content in patients with hepatitis C was significantly reduced. This was interconnected with the severity of their liver disease and the ability of the hepatitis C virus to multiply. The GSH levels were found to be further more lowly in the cases of those who were HIV positive, compared to those with only hepatitis C. Patients addicted to drugs were the one’s to have the lowest GSH levels.

Studies suggested that increased levels of glutathione helps to improve the response to interferon treatment in the cases with hepatitis. It was confirmed that oxidative stress occurred in patients with chronic hepatitis and the studies also showed that the levels of free radicals was correlated with the activity of the hepatitis.

In another study conducted in Italy, improved glutathione levels with high intravenous doses in patients with fatty livers, secondary to alcoholic hepatitis or viral hepatitis (B or C), were marked to show improvement in liver tests, which lasted for several months, after the GSH treatment.

It was found that there was a presence of free radicals due to oxidation of lipids in patients with alcoholic liver disease. Therefore it was concluded that oxidant stress contributes to the deterioration of the liver disease.

Studies made it clear that:

Oxygen and other toxic free radicals, resulting from oxidative stress, occurred in chronic liver disease, which contribute to liver damage in various common types of chronic hepatitis. Levels of antioxidants in blood and liver, mostly those of L-glutathione, are found to be lower in these patients compared to others. Thirdly, higher levels of L-glutathione have shown to improve liver cell damage as reflected by standard liver tests. In chronic hepatitis C, increase of glutathione not only impairs Virus C replication but also renders interferon anti-viral therapy to be more effective.

The studies suggested that the futures of therapy of chronic hepatitis C are likely to include measures to decrease oxidative stress and injury, and the use of multi drug combinations, including inhibitors of hepatitis C virus.

About the Author

MaxGXL has been proven toraise glutathione levels by approximately 250-400% in humans as proven by tests in lymphocytes. MaxGXL provides the proper nutrients needed to promote the body’s own ability to manufacture and absorb glutathione.

This is a demonstration of the Game Speed Hack (GSH.dll) Featured in the Python Suite. **Visit www.ghoztcraft.net or http to get this hack!**

Miami, Florida (PRWEB) August 18, 2011

Nutri-Med Logic Corp: A recent study published in Diabetes Care (2011 July 25), highlighted the importance of R-Alpha Lipoic for the diets of diabetics.

While there are many pharmacological agents with proven efficacy for Diabetic neuropathy (nerve degeneration), but only two nutrients are being closely studies for Painful Diabetic Polyneuropathy: The antioxidant Alpha Lipoic and topical capsaicin, says Diabetes Metabolism Research and Reviews.

Moreover, according to Current Diabetes Report, a longitude of studies, preclinical to clinical, have found a valid relationship between nutritional supplementation of R-Alpha Lipoic and heath benefits in type 2 diabetes.

R-Alpha Lipoic is made by the human body and its levels drop by age. There are functional differences between endogenous (produced by the body) and exogenous (from supplements) R-Alpha Lipoic: Endogenous R-Alpha Lipoic is bound to proteins, whereas the exogenous (supplemental) R-Alpha Lipoic is unattached and easily goes into circulation.

Alpha Lipoic is found in variety of foods but its levels do not increase, significantly, through conventional food and thus its dietary supplementation is the preferred choice for those looking to have its ideal benefits.

Research on R-Alpha Lipoic goes back nearly half of century, when, in 1966, the government of Germany endorsed Alpha Lipoic for Diabetic Polyneuropathy. The first human clinical studies in the United States, relating to R-Alpha Lipoic, were carried out in late 70′s by Dr. Fredrick C. Bartter and Dr. Burton M. Berkson, two associates of the National Institutes of Health. in June 2004, the Ministry of Health, Labor, and Welfare of Japan, also, reclassified Alpha Lipoic as a nutrient.

Additionally, in 1996, an anti-oxidant researcher at University of Berkeley, California, Dr. Packer, a professor of molecular and cell biology discovered that R-Alpha Lipoic also increases the production of and internal anti-oxidant called Glutathione, which re-energizes vitamin C and E. Accordingly, a diet consisting R-Alpha Lipoic not only is beneficial for diabetics, but rather for all.

However, diets of R-Alpha Lipoic for diabetics must be differentiated from diets for those taking R-Alpha Lipoic as an anti-oxidant or in the pursuit of increasing their Glutathione levels, which allow us to conclude that, while, Nutri-Med Logic Corp. agrees with the recent study published in Diabetes Care, but adds that over-supplementation of this nutrient, as any other micro-nutrients, could be worrisome and, in support thereof, sites the landmark study Published by A SPECIAL HEALTH REPORT FROM HARVARD MEDICAL SCHOOL, in 2006, which not only warned against too little of essential micro-nutrient but also against getting too much, as well.

Nutri-Med Logic Corp. believes that unless there is sound and valid reason, more is not better and, to the contrary, more could be worrisome.

Nutri-Med Logic Corp is a producer of dietary supplements, including R-Alpha Lipoic 75mg, which its formulation was based on a sound and logical reasoning: To avoid its over-supplementation, as well as, two years of investigation on the health benefits and the ideal amount of a sustained daily “Dietary Supplementation” of R-Alpha Lipoic.

Nutri-Med Logic’s products are Formulated Based on Nutritional Logic, made from the highest quality raw materials that are manufactured in pharmaceutical facilities, encapsulated in pharmaceutical facilities and, also, packaged in pharmaceutical facilities.

It must be noted that the studies, cited in this release, above or below, have not been evaluated by The FDA and, thus, one should not relate the cause of Diabetes to lack of R-Alpha Lipoic in diet; nor equate supplementation R-Alpha Lipoic to prevention, treatment or cure.

Sources:

Diabetes Care 2011 July 25 [Epub, ahead of print. PubMed ID 21775755]

Diabetes Metabolism Res and Rev. 2011 Jun 21.[Epub ahead of print. PubMed ID 21695762]

Current Diabetes Report. 2011 Apr;11(2):142-8.

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The common name for mercaptan is thiol that literally means mercury capturing. That is a compound which contains an (-SH group) sulfhydryl group. For example, Butyl Mercaptan is called i-ButaneThiol.

Thiols have lower boiling points when compared to alcohols. Thiols show little association by hydrogen bonding, with both water molecules and among themselves. Therefore, they have lower boiling points and are less soluble in water and other polar solvents than alcohols of similar molecular weight.

A common question that may emerge is – which are more acidic: thiols or alcohols? Relative to the alcohols, thiols are fairly acidic.The greater acidity of thiols compared to alcohols can be explained by the fact that sulfur is larger than oxygen. The negative charge on an alkylsulfide ion is delocalized over a larger area and is therefore more stable than the negative charge on an alkoxideion.

Thiols are readily oxidized in the presence of a base by reagents such as iodine to give an organic disulfide (R-S-S-R). For example,2 R-SH + Br2 → R-S-S-R + 2 HBr

Oxidation by more powerful reagents such as sodium hypochlorite or hydrogen peroxide yields sulfonic acids (RSO3H).R-SH + 3H2O2 → RSO3H + 3H2

The role of Thiols in biological molecules is very interesting. The thiol group is critical in the structure of proteins. Proteins are nothing but polyamides — long chains of amino acids linked together by amide links. These chains can coil and take up a variety of shapes, some straight and others snarled like christmas lights. When proteins serve as enzymes (biochemical catalysts), it is essential that the protein have only one shape. Thiols contribute to maintaining that shape.

The functional group of the amino acid cysteine (for instance) is the thiol group which plays an important role in biology. When the thiol groups of two cysteine residues are brought near each other in the course of protein folding, an oxidation reaction can generate a cystine unit with a disulfide bond (-S-S-).

Disulfide bonds can contribute to a protein’s tertiary structure if the cysteines are part of the same peptide chain, or contribute to the quaternary structure of multi-unit proteins by forming fairly strong covalent bonds between different peptide chains.

Sulfhydryl groups in the active site of an enzyme can form noncovalent bonds with the enzyme’s substrate as well, contributing to catalytic activity. Active site cysteine residues are the functional unit in cysteine proteases. Cysteine residues may also react with heavy metal ions (Pb2+, Hg2+, Ag2) because of the high affinity between the soft sulfide and the soft metal. This can deform and inactivate the protein and is one mechanism of heavy metal poisoning.

Small, volatile thiols have a very disagreeable odor. We can look at them as derived from hydrogen sulfide (which smells like rotten eggs). This is similar to the way alcohols are derived from water.

To learn more about thiols and other chemical compounds, go to:http://chemistry.about.comhttp://www.crushthattest.com (flashcards and studyguides on various subjects including chemistry, biology, physics, etc.)http://www.wikipedia.org/wiki/thiols

About the Author

Sundar Nathan received a Bachelor’s degree in Electrical Engineering from Anna University, Chennai, India and a Masters degree in Biomedical Engineering from the University of Texas at Austin. Working for over a year Sundar compiled http://www.crushthattest.com to help students prepare diligently, understand the concepts and Crush that Test!

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Best answer:

Answer by Terrie
Sulphur (in the form of sulphide -SH) is in the amino acid cysteine. When two cysteine amino acids are close enough together they can form disulphide bonds, which is a stong covalent bond between two sulphur atoms (ie, the two hydrogens are removed and are waste products).

This can cause massive stability to the protein as a whole, and affect its structure, which would affect it’s ability to function.

Have a look at this diagram:

http://upload.wikimedia.org/wikipedia/commons/8/82/Disulfide-bond.png

What do you think? Answer below!

Best answer:

Answer by Kate
cysteine amino acids have thiols that are able to form disulfide bridges/bonds. These play a large part in the shape and stability of proteins:

(from Wikipedia):
The disulfide bond stabilizes the folded form of a protein in several ways: 1) It holds two portions of the protein together, biasing the protein towards the folded topology. Expressed differently, the disulfide bond destabilizes the unfolded form of the protein by lowering its entropy. 2) The disulfide bond may form the nucleus of a hydrophobic core of the folded protein, i.e., local hydrophobic residues may condense around the disulfide bond and onto each other through hydrophobic interactions. 3) Related to #1 and #2, the disulfide bond link two segments of the protein chain, the disulfide bond increases the effective local concentration of protein residues and lowers the effective local concentration of water molecules. Since water molecules attack amide-amide hydrogen bonds and break up secondary structure, a disulfide bond stabilizes secondary structure in its vicinity. For example, researchers have identified several pairs of peptides that are unstructured in isolation, but adopt stable secondary and tertiary structure upon forming a disulfide bond between them.

Know better? Leave your own answer in the comments!

This is a preview of The Role of Glutathione in Anti-Aging Medicine by Thomas A. Levy, MD, JD at the 2009A4M Orlando Conference. Visit www.instatapes.com to purchase this lecture and many others on DiGiVision, video and slides syned. Also, visit www.worldhealth.net for the conference sponsor. Item # A4M-091WSS302
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