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L-Glutathione


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#1 luv2increase

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Posted 07 June 2007 - 07:48 PM


Does anyone here supplement L-Glutathione by itself or along with NAC? I'm already taking NAC, and I also thinking about incorporating L-Glutathione into my regimen. What do you all think?


Thanks!
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#2 Shepard

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Posted 07 June 2007 - 10:27 PM

Glutathione is not orally bioavailable.
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#3 luv2increase

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Posted 08 June 2007 - 12:08 AM

Glutathione is not orally bioavailable.



Hmmm. I'm trying to find information of that to back up your claim but can't. Why do they sell l-glutathione if it is useless in supplement form? Will you post something about what you said? Thanks.


Also, I might just start using pomegranate extract instead.


One of my goals is to inhibit melanin production.
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#4 Shepard

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Posted 08 June 2007 - 01:10 AM

1: Eur J Clin Pharmacol. 1992;43(6):667-9.Links
The systemic availability of oral glutathione.
Witschi A, Reddy S, Stofer B, Lauterburg BH.

Department of Clinical Pharmacology, University of Bern, Switzerland.

When the plasma glutathione concentration is low, such as in patients with HIV infection, alcoholics, and patients with cirrhosis, increasing the availability of circulating glutathione by oral administration might be of therapeutic benefit. To assess the feasibility of supplementing oral glutathione we have determined the systemic availability of glutathione in 7 healthy volunteers. The basal concentrations of glutathione, cysteine, and glutamate in plasma were 6.2, 8.3, and 54 mumol.l-1 respectively. During the 270 min after the administration of glutathione in a dose of 0.15 mmol.kg-1 the concentrations of glutathione, cysteine, and glutamate in plasma did not increase significantly, suggesting that the systemic availability of glutathione is negligible in man. Because of hydrolysis of glutathione by intestinal and hepatic gamma-glutamyltransferase, dietary glutathione is not a major determinant of circulating glutathione, and it is not possible to increase circulating glutathione to a clinically beneficial extent by the oral administration of a single dose of 3 g of glutathione.

PMID: 1362956 [PubMed - indexed for MEDLINE]

As for why they sell glutathione as a supplement? Well, the majority of supplements on the market aren't effective.
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#5 luv2increase

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Posted 08 June 2007 - 01:17 AM

or why they sell glutathione as a supplement? Well, the majority of supplements on the market aren't effective.


Yeah, I should have posted that with my post. I realize this. When I see that they gave them a whopping dose of 3g and no significant change, it is good evidence and sufficient to back up what you said.


What do you think about pomegranate in enhancing glutathione shepard?
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#6 Shepard

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Posted 08 June 2007 - 01:26 AM

What do you think about pomegranate in enhancing glutathione shepard?


If boosting GSH is your primary goal, I don't see any reason to go for anything other than NAC. But, I still feel pomegranate juice is worthwhile.
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#7 zoolander

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Posted 08 June 2007 - 05:13 AM

Everything that Shepard said.

Boosting GSH is done quite easily by supplementing with a stable form of cysteine (i.e NAC) or with a cysteine rich protein powder
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#8 albertn

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Posted 08 June 2007 - 03:31 PM

Art Devany seems to think that glutathione is extremely important. He has posted about Glutathione many times on his site and takes a oral version that apparently does reach the cells. (See GlutathioneScience).

I've posted about glutathione a couple of times without any positive reaction. Is it because you don't believe that it can reach the cells via an oral route, or is it because you believe that there are more effective ways of boosting glutathione concentrations (such as taking precursors)?

Assuming it is the former, have any of you looked at Dr. Demopoulos's studies? Assuming it's the latter, can someone post a study that documents the effectiveness of either NAC or whey protein in increasing glutathione?


Albert
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#9 Shepard

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Posted 08 June 2007 - 04:10 PM

Art De Vany is not the most credible source of information. Some of his stuff is worthwhile, some of it isn't. Of course glutathione is important, it's essential for life. Now, glutathione as a supplement isn't.

Considering the lack of impressiveness of that site (slight understatement) and the fact that I find no evidence to consider Dr. Demopoulos an authority of glutathione:

1. Why should I assume his supplement works?
2. Even if it does, why should I use it over other (cheaper) alternatives?

So, why take a chance on something that is more expensive and has extremely questionable effectiveness?

can someone post a study that documents the effectiveness of either NAC or whey protein in increasing glutathione?


Instead of this, I would recommend getting a stronger grasp of glutathione in general. For example, start with understanding glutathione synthesis, what is the rate-limiting step, etc. etc.
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#10 bixbyte

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Posted 08 June 2007 - 07:22 PM

Art De Vany is not the most credible source of information. Some of his stuff is worthwhile, some of it isn't. Of course glutathione is important, it's essential for life. Now, glutathione as a supplement isn't.

Considering the lack of impressiveness of that site (slight understatement) and the fact that I find no evidence to consider Dr. Demopoulos an authority of glutathione:

1. Why should I assume his supplement works?
2. Even if it does, why should I use it over other (cheaper) alternatives?

So, why take a chance on something that is more expensive and has extremely questionable effectiveness?

can someone post a study that documents the effectiveness of either NAC or whey protein in increasing glutathione?


Instead of this, I would recommend getting a stronger grasp of glutathione in general. For example, start with understanding glutathione synthesis, what is the rate-limiting step, etc. etc.



Each of your cells should contain 5 mmol of Gluthione.
Glutathione has more potential then Resveratrol.
But, would be preaching to the wrong flock if I posted that last statement?

Alex Kalman
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#11 Shepard

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Posted 08 June 2007 - 07:36 PM

I don't get it.
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#12 krillin

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Posted 08 June 2007 - 07:50 PM

can someone post a study that documents the effectiveness of either NAC or whey protein in increasing glutathione?


Whey and NAC are about the same at increasing glutathione, but whey has additional benefits that NAC lacks.

Toxicol In Vitro. 2003 Feb;17(1):27-33.
Effect of whey protein isolate on intracellular glutathione and oxidant-induced cell death in human prostate epithelial cells.
Kent KD, Harper WJ, Bomser JA.

Department of Food Science and Technology, The Ohio State University, 2015 Fyffe Road, Columbus, OH 43210, USA.

Cysteine is the rate-limiting amino acid for synthesis of the ubiquitous antioxidant glutathione (GSH). Bovine whey proteins are rich in cystine, the disulfide form of the amino acid cysteine. The objective of this study was to determine whether enzymatically hydrolyzed whey protein isolate (WPI) could increase intracellular GSH concentrations and protect against oxidant-induced cell death in a human prostate epithelial cell line (designated RWPE-1). Treatment of RWPE-1 cells with hydrolyzed WPI (500 microg/ml) significantly increased intracellular GSH by 64%, compared with control cells receiving no hydrolyzed WPI (P<0.05). A similar increase in GSH was observed with N-acetylcysteine (500 microM), a cysteine-donating compound known to elevate intracellular GSH. In contrast, treatment with hydrolyzed sodium caseinate (500 microg/ml), a cystine-poor protein source, did not significantly elevate intracellular GSH. Hydrolyzed WPI (500 microg/ml) significantly protected RWPE-1 cells from oxidant-induced cell death, compared with controls receiving no WPI (P<0.05). The results of this study indicate that WPI can increase GSH synthesis and protect against oxidant-induced cell death in human prostate cells.

PMID: 12537959

J Nutr Biochem. 2006 Dec 1;
Meal cysteine improves postprandial glucose control in rats fed a high-sucrose meal.
Blouet C, Mariotti F, Mikogami T, Tome D, Huneau JF.

UMR 914 INRA, INAPG, Nutrition Physiology and ingestive behavior, Institut National Agronomique, Paris 75005, France.

Whey protein, particularly the alpha-lactalbumin fraction, are rich in cysteine (cys) and could therefore favor postprandial glucose homeostasis by a glutathione-mediated effect. This work investigates the effects of the ingestion of an alpha-lactalbumin-rich whey concentrate (alpha-LAC) during a high-sucrose (HS) meal on postprandial glucose homeostasis in healthy rats. In the first experiment, rats received an HS meal containing 14% protein, in which the protein source was either alpha-LAC (HS(a)) or total milk proteins, alone (HS(0)) or supplemented with 17 mg (HS(1)) or 59 mg (HS(2)) of N-acetylcysteine (NAC). This resulted in a total cys content 3.6-fold higher in the HS(1) and HS(a) meals and 12-fold higher in the HS(2) meal, when compared to the HS(0) meal. Postprandial parameters were monitored for 3 h after ingestion of the meal. The same measurements were performed on rats injected with 4 mmol/kg of buthionine sulfoximine (BSO), a specific inhibitor of glutathione synthesis. Increasing the meal's cys content dose-dependently reduced both postprandial glucose and insulin (P<.05). The inhibition of glutathione synthesis with BSO injection abrogated the beneficial effects of NAC supplementation on postprandial glucose response but did not affect those of alpha-LAC. These results show that (1) the substitution of alpha-LAC for total milk protein reduces glucose response, as does the addition of a cys donor to the meal, (2) but contrary to those of a simple cys donor, the beneficial effects of alpha-LAC are not entirely mediated by glutathione synthesis, suggesting additional mechanisms.

PMID: 17142027
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#13 bixbyte

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Posted 08 June 2007 - 07:59 PM

Glutathione

DESCRIPTION
The term glutathione is typically used as a collective term to refer to the tripeptide L-gamma-glutamyl-L-cysteinylglycine in both its reduced and dimeric forms. Monomeric glutathione is also known as reduced glutathione and its dimer is also known as oxidized glutathione, glutathione disulfide and diglutathione. In this monograph, reduced glutathione will be called glutathione— this is its common usage by biochemists—and the glutathione dimer will be referred to as glutathione disulfide.

Glutathione is widely found in all forms of life and plays an essential role in the health of organisms, particularly aerobic organisms. In animals, including humans, and in plants, glutathione is the predominant non-protein thiol and functions as a redox buffer, keeping with its own SH groups those of proteins in a reduced condition, among other antioxidant activities. Glutathione has the following structural formula:

Glutathione is present in tissues in concentrations as high as one millimolar. Cysteine, the business residue of glutathione, neither has the solubility nor activity of glutathione at physiological pH. It appears that nature has built the cysteine molecule into the glutathione tripeptide to make the amino acid more soluble and allow it to have redox buffering activity in a living tissue environment. Glutathione also plays roles in catalysis, metabolism, signal transduction, gene expression and apoptosis. It is a cofactor for glutathione S-transferases, enzymes which are involved in the detoxification of xenobiotics, including carcinogenic genotoxicants, and for the glutathione peroxidases, crucial selenium-containing antioxidant enzymes (see Selenium). It is also involved in the regeneration of ascorbate from its oxidized form, dehydroascorbate (see Vitamin C). There are undoubtedly roles of glutathione that are still to be discovered.

Glutathione is present in the diet in amounts usually less than 100 milligrams daily, and it does not appear that much of the oral intake is absorbed from the intestine into the blood (see Pharmacokinetics). Glutathione is not an essential nutrient since it can be synthesized from the amino acids L-cysteine, L-glutamate and glycine. It is synthesized in two ATP-dependent steps: first, gamma-glutamylcysteine is synthesized from L-glutamate and cysteine via the enzyme gamma-glutamylcysteine synthetase—the rate limiting step— and second, glycine is added to the C-terminal of gamma-glutamylcysteine via the enzyme glutathione synthetase. The liver is the principal site of glutathione synthesis. In healthy tissue, more than 90% of the total glutathione pool is in the reduced form and less than 10% exists in the disulfide form. The enzyme glutathione disulfide reductase is the principal enzyme that maintains glutathione in its reduced form. This latter enzyme uses as its cofactor NADPH (reduced nicotinamide adenine dinucleotide phosphate). NADPH is generated by the oxidative reaction in the pentose phosphate pathway.

The consequences of a functional glutathione deficiency, which results in tissue oxidative stress, can be seen in some pathological conditions. For example, those with glucose 6-phosphate dehydrogenase deficiency produce lower amounts of NADPH and hence, lower amounts of reduced glutathione. This condition is characterized by a hemolytic anemia. Conditions causing chronic glutathione deficiency all result in hemolytic anemia, among other pathological consequences. Oxidative stress caused by glutathione deficiency results in fragile erythrocyte membranes. Malaria-causing organisms (Plasmodia species) do not like to feed on these sick erythrocytes. That is about the only good news regarding this situation. Chronic functional glutathione deficiency is also associated with immune disorders, an increased incidence of malignancies, and in the case of HIV disease, probably accelerated pathogenesis of the disease. Acute manifestations of functional glutathione deficiency can be seen in those who have taken an overdosage of acetaminophen. This results in depletion of glutathione in the hepatocytes, leading to liver failure and death, if not promptly treated.

Glutathione is an orphan drug for the treatment of AIDS-associated cachexia. It is thought that this disorder is due, in part, to oxidatively-stressed and damaged enterocytes. There is some evidence that although orally administered glutathione may not be absorbed into the blood from the small intestine to any significant extent, that it may be absorbed into the enterocytes where it may help repair damaged cells. Glutathione in one form or another is the subject of some medicinal chemistry research and some clinical trials. For example, an aerosolized form of glutathione is being studied in AIDS and cystic fibrosis patients. Glutathione, the principal antioxidant of the deep lung, appears to be diminished in those with AIDS. Prodrugs of gamma-L-glutamyl-L-cysteine are being evaluated as anticataract agents.

Glutathione (reduced) is known chemically as N-(N-L-gamma-glutamyl-L-cysteinyl)glycine and is abbreviated as GSH. Its molecular formula is C10H17N3O6S and its molecular weight is 307.33 daltons. Glutathione disulfide is also known as L-gamma-glutamyl-L-cysteinyl-glycine disulfide and is abbreviated as GSSG. Its molecular formula is C20H32N6O12S2.

The marketed glutathione dietary supplement products are obtained from yeast fermentation, as is the orphan drug. L-Cysteine and N-acetylcysteine are precursors of glutathione and are also available as dietary supplements (see L-Cysteine and N-Acetylcysteine).

ACTIONS AND PHARMACOLOGY
ACTIONS
Glutathione has antioxidant activity. It may have detoxification, and immunomodulatory activities, and may have beneficial effects on sperm motility and in the protection against noise-induced hearing loss.

MECHANISM OF ACTION
Glutathione is the principal intracellular non protein thiol and plays a major role in the maintenance of the intracellular redox state. It may be thought of as an intracellular redox buffer. Glutathione is a nucleophilic scavenger and an electron donor via the sulfhydryl group of its business residue, cysteine. Its reducing ability maintains molecules such as ascorbate and proteins in their reduced state. Glutathione is also the cofactor for the selenium-containing glutathione peroxidases (see Selenium), which are major antioxidant enzymes. These enzymes detoxify peroxides, such as hydrogen peroxide and other peroxides. Another antioxidant activity of glutathione is the maintenance of the antioxidant/reducing agent ascorbate in its reduced state. This is accomplished via glutathione-dependent dehydroascorbate reductase which is comprised of glutaredoxin and protein isomerase reductase. Glutathione may also react with the reactive nitrogen species peroxynitrite to form S-nitrosoglutathione.

Glutathione S-transferases (GSTs) consist of a family of multifunctional enzymes that metabolize a wide variety of electrophilic compounds via glutathione conjunction. GSTs are involved in the detoxification of xenobiotic compounds and in the protection against such degenerative diseases as cancer. The mechanism of these enzymes involves a nucleophilic attack by glutathione on an electrophilic substrate. The resulting glutathione conjugates that form are more soluble than the original substrates and thus more easily exported from the cell. The release of glutathione-S-conjugates from cells is an ATP-dependent process mediated by membrane glycoproteins belonging to the multidrug-resistance protein (MRP) family. Proteins of the MRP family are essential for the transport of glutathione S-conjugates into the extracellular space. They are also known as glutathionine-S-conjugate pumps.

Absorption of orally administered glutathione has been observed in some animals (mice, rats, guinea pigs). Oral glutathione has been demonstrated to reverse age-associated decline in immune responsiveness in mice. In one study, glutathione was found to enhance T-cell mediated responsiveness, including delayed-type hypersensitivity (DTH). The mechanism of this effect was ascribed to the antioxidant activity of glutathione.

Parenterally administered glutathione was found to improve sperm motility in a small human trial. Again, the effect was thought to be due to the antioxidant activity of this substance.

Noise-induced hearing loss is thought to be due to oxidative stress. Intraperitoneal administration of glutathione to guinea pigs was found to protect against noise-induced hearing loss and once more, the antioxidant activity of glutathione was thought to account for this effect.
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#14 bixbyte

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Posted 08 June 2007 - 08:01 PM

PHARMACOKINETICS

The pharmacokinetics of oral glutathionine in humans are not well understood. It appears that in some animals (mice, rats, guinea pigs), serum glutathione levels do increase following its oral administration. Most human studies of glutathione have not found this to be the case. It appears that oral glutathione is hydrolyzed in the intestine via the intestinal gamma-glutamyl transferase enzyme. A small amount of orally administered glutathione may reach the portal circulation, but apparently this is also rapidly metabolized by hepatic gamma-glutamyltransferase. Thus, most studies have not observed a significant increase in circulating glutathione following its oral administration. However, there is an occasional study that does show an increase in circulating glutathione after oral administration. Further, there is some evidence that glutathione may be absorbed into the enterocytes following ingestion, but may not be released by these cells into the circulation. Research is needed to resolve the issue of glutathione absorption.
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#15 bixbyte

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Posted 08 June 2007 - 08:07 PM

PHARMACOKINETICS

The pharmacokinetics of oral glutathionine in humans are not well understood. It appears that in some animals (mice, rats, guinea pigs), serum glutathione levels do increase following its oral administration. Most human studies of glutathione have not found this to be the case. It appears that oral glutathione is hydrolyzed in the intestine via the intestinal gamma-glutamyl transferase enzyme. A small amount of orally administered glutathione may reach the portal circulation, but apparently this is also rapidly metabolized by hepatic gamma-glutamyltransferase. Thus, most studies have not observed a significant increase in circulating glutathione following its oral administration. However, there is an occasional study that does show an increase in circulating glutathione after oral administration. Further, there is some evidence that glutathione may be absorbed into the enterocytes following ingestion, but may not be released by these cells into the circulation. Research is needed to resolve the issue of glutathione absorption.



"PharmacoKinetics"

"However, there is an occasional study that does show an increase in circulating glutathione after oral administration. "



Like I posted, you may be able to absorb Glutatione sublingually.
I have been leaving a couple 100 MG under my tongue and in my cheeks for years.

Alex Kalman
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#16 bixbyte

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Posted 08 June 2007 - 08:10 PM

RESEARCH SUMMARY
The use of glutathione in cancer treatment has been two-fold. It has been investigated as an antitumor agent in its own right and as a chemoprotectant used to diminish the toxicities of some cancer drugs. In one animal study, glutathione produced significant regression of aflatoxin-induced liver cancers and significantly enhanced survival. All rats exposed to aflatoxin but not given glutathione died within 24 months of exposure to the carcinogen, but 81% of the glutathione-treated animals were still alive at the end of the 24 months. The researchers concluded that the glutathione-effect noted in this study "strongly suggests that this antioxidant merits further investigation as a potential antitumor agent in humans."

Human cancer studies, so far, have utilized glutathione in a secondary role—principally to protect against the toxicity of cisplatin. Its role in this regard has been found effective in several studies wherein it has been demonstrated to diminish cisplatin-induced nephrotoxicity and neurotoxicity.

Early research indicates that exogenous glutathione may significantly inhibit platelet aggregation and improve other hemostatic and hemorheological factors in atherosclerotic patients. In other preliminary clinical work, glutathione has been found to help preserve renal function in patients who had coronary artery bypass operations.

A glutathione aerosol preparation has been helpful in reversing the oxidant-antioxidant imbalance in idiopathic pulmonary fibrosis, and it has helped suppress lung epithelial surface inflammatory cell-derived oxidants in patients with cystic fibrosis. Similar aerosol treatment has been given to HIV patients to augment deficient glutathione levels of the lower respiratory tract with the idea of improving host defense in these immuno-compromised individuals. More research is needed.

Glutathione has also been shown to enhance insulin secretion in elderly subjects with impaired glucose tolerance. There are some further preliminary indications that glutathione might be helpful in some with diabetes, but more research is needed before any meaningful conclusions can be made.

In a double-blind, placebo-controlled study, injected glutathione demonstrated a significant positive effects on sperm motility and morphology in infertile men. And, finally, in another study that needs followup, glutathione exhibited significant in vitro inhibition of herpes simplex virus type 1 replication. It appears that the mechanism of this effect is due to glutathione's redox-modulating active. Some viral infections, including HIV infection, result in oxidative stress which may be a major mechanism of their pathogenesis, Modulating oxidative stress could be an antiviral maneuver.
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#17 Shepard

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Posted 08 June 2007 - 08:11 PM

Like I posted, you may be able to absorb Glutatione sublingually.


Let's assume sublingual glutathione is effective. So if we attempt this directly, we've got sublingual, IV, and/or nebulous treatments.

What is your argument for this method instead of precursor supplementation?
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#18 luv2increase

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Posted 08 June 2007 - 08:38 PM

Like I posted, you may be able to absorb Glutatione sublingually.


Let's assume sublingual glutathione is effective. So if we attempt this directly, we've got sublingual, IV, and/or nebulous treatments.

What is your argument for this method instead of precursor supplementation?


There is no argument, I have been using everyway possible to increase my Glutathione levels as high as possible.
I might go subcutaneously too.


Alex Kalman


Do you use NAC also? Is it possible to have too much of a good thing such as glutathione?
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#19 Shepard

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Posted 08 June 2007 - 08:52 PM

Is it possible to have too much of a good thing such as glutathione?


I would lean between very likely to absolutely.
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#20 bixbyte

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Posted 08 June 2007 - 09:01 PM

Like I posted, you may be able to absorb Glutatione sublingually.


Let's assume sublingual glutathione is effective. So if we attempt this directly, we've got sublingual, IV, and/or nebulous treatments.

What is your argument for this method instead of precursor supplementation?


There is no argument, I have been using everyway possible to increase my Glutathione levels as high as possible.
I might go subcutaneously too.


Alex Kalman


Do you use NAC also? Is it possible to have too much of a good thing such as glutathione?


Yes, I take 600 Mg of NAC daily.
I do know that hundred year olds have high levels of Glutathione.
I also know some uses for Glutathione that have not been studied yet in the USA

Alex Kalman
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#21 bixbyte

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Posted 08 June 2007 - 09:08 PM

Is it possible to have too much of a good thing such as glutathione?


I would lean between very likely to absolutely.


Do you have any references?
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#22 Shepard

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Posted 08 June 2007 - 09:45 PM

Do you have any references?


The topic is vast. I don't pretend to be all-knowing about it, but if you'll begin to look into what role hydrogen peroxide plays in the body you'll probably understand where I'm coming from.

If you're seriously interested, I'd recommend trying to find a copy of this book: http://www.amazon.co...81338904&sr=8-1
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#23 bixbyte

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Posted 09 June 2007 - 05:49 AM

Do you have any references?


The topic is vast. I don't pretend to be all-knowing about it, but if you'll begin to look into what role hydrogen peroxide plays in the body you'll probably understand where I'm coming from.

If you're seriously interested, I'd recommend trying to find a copy of this book: http://www.amazon.co...81338904&sr=8-1




I have studied Glutathione uses very closely for the last couple years.
But, I am not an expert on the Thermodynamics of cellular reactions of Glutathionization.
I understand what you getting at as a hydrogen peroxide electron positive reaction.
In my opinion more important would be efficacy studies and the most important would be toxcitity/safety studies on humans of Glut.
I was reding over the content provided by Amazon.com. If the book was less money I'd read it over.

I have been dosing myself with various products that might raise my Glutathione levels for a couple of years.
I could explain to you why, but you probably would not be interested.
You are looking for longevity and I am looking for cell protection.

Good Luck,

Alex Kalman
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#24 zoolander

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Posted 09 June 2007 - 07:23 AM

A scientific study published in a peer reviewed and reliable medical journal was quoted at the very start of this thread. This study concluded....

Because of hydrolysis of glutathione by intestinal and hepatic gamma-glutamyltransferase, dietary glutathione is not a major determinant of circulating glutathione, and it is not possible to increase circulating glutathione to a clinically beneficial extent by the oral administration of a single dose of 3 g of glutathione.


hence oral supplementation with glutathione is not advised. Now Alex, you use glutathione sublingually. This may or may not work. There is currently no published studies out there to demonstrate this. At least none that I have seen. Glutathione is a very important thiol and if it's bioavailability was increased by using sublingual glutathione then I'm betting that someone would have published something.

Instead though it has been shown on many occasions that increasing cysteine levels is a very effective method by which you can increase inracellular glutathione. Dietary cysteine comes from NAC and cysteine rich whey protein powders.

For some reason it seems as though you believe that sublingual glutathione works. That's fine of course but research shows that you are wasting your money and could be using cheaper alternatives.

I have been dosing myself with various products that might raise my Glutathione levels for a couple of years.
I could explain to you why, but you probably would not be interested.


Please tell us Alex because

You are looking for longevity and I am looking for cell protection.


are essentially the same thing.
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#25 bixbyte

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Posted 09 June 2007 - 03:12 PM

A scientific study published in a peer reviewed and reliable medical journal was quoted at the very start of this thread. This study concluded....



hence oral supplementation with glutathione is not advised. Now Alex, you use glutathione sublingually. This may or may not work. There is currently no published studies out there to demonstrate this. At least none that I have seen. Glutathione is a very important thiol and if it's bioavailability was increased by using sublingual glutathione then I'm betting that someone would have published something.

Instead though it has been shown on many occasions that increasing cysteine levels is a very effective method by which you can increase inracellular glutathione. Dietary cysteine comes from NAC and cysteine rich whey protein powders.

For some reason it seems as though you believe that sublingual glutathione works. That's fine of course but research shows that you are wasting your money and could be using cheaper alternatives.

I have been dosing myself with various products that might raise my Glutathione levels for a couple of years.
I could explain to you why, but you probably would not be interested.


Please tell us Alex because



are essentially the same thing.


First of all, I am afraid to post this to you.

If I reveal this tidbit of info, shall I receive any credit or references for my knowledge?

Alex Kalman
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#26 zoolander

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Posted 09 June 2007 - 10:37 PM

So essentially you are suggesting that you arethe first to use/do whatever you are doing?
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#27 luv2increase

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Posted 10 June 2007 - 02:17 AM

A scientific study published in a peer reviewed and reliable medical journal was quoted at the very start of this thread. This study concluded....



hence oral supplementation with glutathione is not advised. Now Alex, you use glutathione sublingually. This may or may not work. There is currently no published studies out there to demonstrate this. At least none that I have seen. Glutathione is a very important thiol and if it's bioavailability was increased by using sublingual glutathione then I'm betting that someone would have published something.

Instead though it has been shown on many occasions that increasing cysteine levels is a very effective method by which you can increase inracellular glutathione. Dietary cysteine comes from NAC and cysteine rich whey protein powders.

For some reason it seems as though you believe that sublingual glutathione works. That's fine of course but research shows that you are wasting your money and could be using cheaper alternatives.

I have been dosing myself with various products that might raise my Glutathione levels for a couple of years.
I could explain to you why, but you probably would not be interested.


Please tell us Alex because



are essentially the same thing.


First of all, I am afraid to post this to you.

If I reveal this tidbit of info, shall I receive any credit or references for my knowledge?

Alex Kalman


Come on. Quit holding out on this great information. You just may be on to the GFOY (glutathione fountain of youth). Don't be stingy and reveal your secrets. You are among friends here.
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#28 Shepard

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Posted 10 June 2007 - 03:53 AM

Oh, dear lord sweet baby Jesus.
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#29 zoolander

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Posted 10 June 2007 - 04:21 AM

Shep, agreed. The oxidized glutathione (GSSG) is the by product the reaction and not the catalyst. Your supplementing with the wrong end my friend.

Reduced glutathione (GSH) acts as the substrate in the reaction and is used to neutralize hydrogen peroxide via glutathione peroxidase (GPx) or catalase.

I can tell you from first hand experience because I have measured changes in plasma cysteine and intracellular reduced, oxidized and Total Glutathione in aged male that whey protein supplementation is sufficient enough to increase one's GSH level and hence change the redox status of the cell minimizing oxidative stress.

To increase GSH levels you can also supplement with alpha-lipoic acid
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#30 bixbyte

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Posted 10 June 2007 - 05:34 AM

Shep, agreed. The oxidized glutathione (GSSG) is the by product the reaction and not the catalyst. Your supplementing with the wrong end my friend.

Reduced glutathione (GSH) acts as the substrate in the reaction and is used to neutralize hydrogen peroxide via glutathione peroxidase (GPx) or catalase.

I can tell you from first hand experience because I have measured changes in plasma cysteine and intracellular reduced, oxidized and Total Glutathione in aged male that whey protein supplementation is sufficient enough to increase one's GSH level and hence change the redox status of the cell minimizing oxidative stress.

To increase GSH levels you can also supplement with alpha-lipoic acid


Mr Zoo and Shep,

Very good and written scientifically too.
Yes and I take ALA daily.
Feed me on the supplementing end, raise my Glutathione levels higher, how?
Please Illuminate us.

Thank You,

Alex Kalman
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