The scoop on whey's anti-aging power

As Gustavo Bounous' book "Glutathione: Your Body's Most Powerful Healing Agent" points out, regular uncooked whey increases production of your master antioxidant and detoxifier glutathione. In animal studies, undenatured whey protein consistently raised glutathione levels beyond those of any other protein studied, including soy (Bounous G. and Gold P., Clin. Invest. Med. 1991). 

Glutathione is an essential water-soluble antioxidant that protects cells and neutralizes free radicals and toxins such as peroxides, heavy metals, carcinogens, and many others. Glutathione is part of the cellular energy cycle; when levels are low you get reduced ATP production, cell wasting and cell death. Glutathione is so necessary to a healthy immune system that it appears immunity itself can be modulated by glutathione levels (Rosanne K., Fidelus and Min Fu Tsan. Cellular Immunology, 1986). 

When your body's most powerful healing agent is low you are sick, even when the other antioxidants are replete. Even vitamin C can't save you if your glutathione is low. Conversely, one survives low vitamin C and other antioxidants because they are recycled by glutathione rather than wasted after a single use. Disease, degeneration, and infection are stimulated by low glutathione, while high glutathione is associated with wellness. 


Health-conscious individuals around the world use cold-processed whey protein as a daily part of an anti-aging or health program to maintain glutathione levels and body mass index. Just 25-30 grams of udenatured whey isolate or 35-40 grams of concentrate is an adequate dose to produce glutathione, with the dose doubling or tripling for body building and in illness. Undenatured whey produces an alkalizing rather than an acidifying effect that is attributed to most proteins; it also requires the least digestion of any protein, which makes it an excellent protein choice for those whose digestion is impaired, and for the very young, especially formula-fed babies, and for those who need to avoid kidney nitrogen loading. Cold-processed whey may be the missing ingredient in your program. 

octors and health professionals recommend cold processed whey because it is the ideal glutathione precursor, and feedback from users of this fundamental, science-based approach underscores its validity. This supplement is of particular importance for people with inflammation for example in Crohn's disease, (CD) or ulcerative colitis, (UC) or any variant of inflammatory bowel disease (IBD); irritable bowel syndrome (IBS); candida; arthritis or any other itis, which means inflammation. In fact glutathione may be completely depleted at the injured site. 


See some of the diseases that are linked to low glutathione in these prewritten queries: glutathione references on PubMed. The approach is both well-backed by science and well-proven in practice. If your glutathione levels are low, ANY other therapy will probably fail; it is that fundamental.

Selenium is crucial for making glutathione peridoxase. Healthy people could use 200 mcg daily, but those who are sick or have a degenerative illness could use more. The US Department of Agriculture suggests North Amercian adults should supplement with 150 mcg daily, and notes that the consumption of Se in amounts that exceed the Recommended Dietary Allowance (RDA) may protect against prostate and colorectal cancer. Reduce selenium depletion also by reducing your exposure to arsenic in drinking water. While selenium's therapeutic window is 200-600 mcg daily, cancer and viral studies used 1,100 mcg. Selenium is toxic but 3,200 mcg taken daily for a year produced only deformed fingernails, which soon grew out.


Comparing glutathione-producing undenatured wheys

Bonded cysteine is the rate-limiting factor for glutathione production. You can determine how much bonded cysteine is in an undenatured whey from its components: serum albumin; alpha-lactalbumin; beta-lactoglobulin; lactoferrin. There are 17 cystine residues and six Glu-Cys dipeptides (Eigel et al, 1984) per 66,000 MW molecule of serum albumin; 17 cystine residues and four Glu-Cys dipeptides per 77,000 MW molecule (Goodman and Schanbacher, 1991) in Lactoferrin; four cystine residues per 14,000 MW molecule (Eigel et al, 1984) in Alpha-Lactalbumin. Beta-lactoglobulin contains two cystine residues per 18,400 MW molecule (Eigel et al, 1984), and IgG1, the predominant immunoglobulin in cows milk serum, only four disulfide bridges (cysteine) per 166,000MW molecule (Baruchel et al, 1996). Each cystine residue is TWO cysteines in bonded, bioavailable form.

So, to know what you're getting you have to compare the actual components of the protein. Some wheys list the protein fractions as a percentage of total protein, while others list their protein fractions in mg from a 25-g scoop, 30-g or 36 gram scoop etc. if they list them at all. Different extraction and pasteurization techniques yield varying protein fractions and varying degrees of breakage (denaturing) of the delicate peptides. 

The cysteine reading on a whey label can be misleading because denaturing may have been broken up the bonded cysteine, leaving the free form amino acid, which is ineffective. Free cysteine is also toxic (Meister, 1984; Baruchel et at., 1996) and is poorly absorbed and transported; N-acetyl-L-cysteine (NAC), an amine protected pharmaceutical version of cysteine, is rapidly hydrolyzed in the body to cysteine and it has a very short half-life. 

If you don't want to work it out you have to have a bit of good faith in the manufacturer or good faith in the label. I prefer the manufacturer that touts their low temperature extraction process in general and careful preservation of glutathione-producing peptides in particular.