Lactoferrin is an iron-binding, iron-modulating protein which is found in bovine milk and has greater existence in our whey protein concentrate. Lactoferrin resides in the chemical family called cytokines. This family of chemicals coordinates the body's cellular immune defensive response that protects us from most infections, tumors, and cancers. They additionally boost the activity of T-cells, as well as stimulate production of immunoglobulins. Without these cytokines our immune system suffers and reacts by creating an over-active immune response. It is our body's first defense to protect orifices such as the eyes, mouth, and nose from bacterial infection.

Lactoferrin and Iron Modulation

Lactoferrin is an essential bioactive molecule which can provide iron to those cells in need, as well as limit it to those in excess, maintaining an iron homeostasis within the body.
Iron deficiency is a fairly common disorder; it affects billions of people a year. The deficiency of iron can lead to extreme anemia, characterized by fatigue, lethargy, heart palpitations, and shortness of breath. The role of iron in a well functioning body and immune system is well documented and much agreed upon across the board. Common sufferers of iron deficiency include (but are not limited to) women, children, vegetarians, as well many studies conclude, high endurance athletes. The body does not easily assimilate iron (or lactoferrin) in a denatured state (highly processed) which is how it is presented in many bovine dietary supplements. With these supplements high amounts are required for any benefit to arise. Healthy Planet Vitamins is a non-denatured whey protein supplement

that is not a by-product of cheese manufacturing and therefore the bioavailability of the lactoferrin is maintained.

However, excess iron is a risk as well, although not as common. Some complications associated with this disorder are: bacterial infections, diarrhea, gastrointestinal disorders, and even iron-toxicity. Several of these complications arise from the body’s ingestion of unbound iron. Iron that is bound to lactoferrin is much easier to absorb in the body and utilize, and is not lost through human excretions or through other organisms in the body. Iron not bound in the body is a catalyst for the production of free radicals, which have a negative effect on the body’s biology. Lactoferrin is an important part of the body's natural defense. Studies show that it inhibits the binding of pathogens like H. pylori and E. coli to the intestinal wall. Many micro-organisms need iron for growth, by limiting the levels of free iron; lactoferrin can inhibit bacterial growth and assist to deprive them of iron. The pathogens cellular structure loses its integrity because of the iron deprivation and necrosis ensues.

Lactoferrin Studies

The first major entrance of lactoferrin in the health industry was prompted by a paper written by an AIDS researcher discussing the importance of lactoferrin as a regulator of the immune response in people with AIDS. Recent studies have shown that lactoferrin can also inhibit the growth of the HIV virus.

There have been several; studies proving lactoferrin to be an extremely beneficial substance. The antibacterial properties have been well documented. A study by the Institute of Public Health in Tokyo, Japan showed that E. coli 0157:H7 can falter under influence of the anti microbial effects of bovine lactoferrin. Another well documented study by the National Cancer Institute in Tokyo, Japan concluded that bovine lactoferrin inhibits the Hepatitis C infection in human cells. This is of major importance for Hepatitis C has been found to be the main causative factor in chronic viral hepatitis. Lactoferrin seems to inhibit the absorption of the viral particle to the human cell by binding to the cell receptor site or to the virus.


Lactoferrin has a broad range of benefits, it enhances and modulates immune-function overall, as well as has many iron-enhancing and modulating benefits. Furthermore, it has been said to act as an immunostimulating factor in the digestive system, as well as an inhibitor of the growth of many unhealthy micro-organisms in the digestive tract. Lactoferrin regulates the immune response of the body in many differing ways. It inhibits many viruses from thriving in the body and is essentially an important component in immune-therapy. Healthy Planet Vitamins provides an excellent source of non-denatured lactoferrin in its most biologically available state.


Immunoglobulins (IgG) are proteins that are present in bovine whey protein. One of their functions is as a transporter of antibodies against harmful microorganisms like viruses, bacteria's, and other foreign invaders. IgG has been used to treat diseases such as multiple sclerosis, rheumatoid arthritis, hepatitis A, anemia, Chronic Fatigue Syndrome, and chickenpox, among others. IgG are essential elements in maintaining a humans immunity from detrimental microorganisms and toxins. This substance is transferred from mother to child inside of the womb via the mother’s blood to protect him/her from the introduction of pathogens in the outside world. This way the child is born with a passive immunity. IgG works together and separately to battle antigens. They circulate in the blood and lymphatic systems or they reside in the mucous membranes to act as a barrier against invaders.

These immunoglobulins are of a critical importance because several bacteria's become more resistant to antibiotics every day. These bacteria infect our food supply and there are more viruses created at a faster rate than the vaccines used to battle them, science consistently has to catch up. More and more diseases are being linked to bacterial infection, including peptic ulcers and heart disease. In fact, there is strong evidence linked between bacterial infection and heart disorders. (1).Healthy Planet Vitamins with their high amounts of IgG plays a role in the combat or these elements.

How The Body Utilizes IgG

Our body's first line of immune defense to unhealthy organisms is through the intestinal tract (2). The IgG has been found to resist break down by the digestive enzymes within the digestive tract (due to the glycoprotein’s and trypsin inhibitors), therefore the IgG enters the intestinal wall fully intact where they defend the lining against invading organisms, and prevent the absorption of foreign proteins. The IgG is a factor in increasing the immune system activity level. This substance is vital in stabilizing and restoring a damaged intestinal tract so it can function at its optimum capacity for nutrient absorption and utilization.

The antibodies derived from bovine milk have many of the mothers milk IgG characteristics and may be active against the same diseases in humans. Immunoglobulins consist of four polypeptide chains with two of the same heavy chains linked by covalent and non-covalent bridges. The light and heavy chains both have areas with constant amino acids and with a variable region. This variable region is where the antibody meets the antigen (foreign molecule). The bovine milk antigens are resistant to the peptic digestion processes, which is essential for using a non-denatured whey protein abundant in IgG proteins (3).


 1. G. Bauriedel, et al.Chlamydia pnuemoniae in coronary plagues. Increased detection with acute coronary syndrome. Dtsch Med Wochenssch 124(13) (April 1, 1999): 37-80; FL Visseren, et al. Atherosclerosis as an infectious disease. Ned Tijdschr Geneeskdl 143(6) (Feb 6, 1999): 291-95; J. Danesch, et al. Is helicobacter pylori a factor in atherosclerosis? J Clin Microbiol 37(5) )May, 1999): 1651; Dp Strachan, et al., Relation of Chlamydia pneumonia serology to mortality and incidence of ischaemic over 13 years in the caerphilly prospective heart disease study. Br Med J 318(7190) (April 17, 1999): 1035-39; Norman Watner, The Salt lake Tribune June 1, 1996.

2. Guyton AC. Protein Metabolism. In: Textbook of Medical Physiology 8th edition. Philadelphia (PA): WB Saunders; 1991.

3. Watson DL. Immunologic functions of the mammary gland and its secretion - Comparative review. Aust J Biol Sci 1980; 33:402-422

Glutathione Benefits

Immune System
In the fight against disease, immune depressed individuals have lower GSH levels. Lymphocytes, cells vital for your immune response, depend on GSH for their proper function and replication. Immunology 61: 503-508 1987. Cellular depletion of Glutathione has been implicated as a cause, or contributory factor in many pathologies including Parkinson's, Alzheimer's, cataracts, arteriosclerosis, cystic fibrosis, malnutrition, aging, AIDS, and cancer (Bounous et al., 1991). In addition, Glutathione is vital in supporting the immune system, including natural killer cells (Droege et al., 1997), as well as the maintenance of T-lymphocytes (Gutman, 1998).

GSH plays a role in eliminating many carcinogens, as well as maintaining immune function towards providing stronger anti-tumor defenses. Cancer Letters 57: 91-94 1991

Aging Process
It is well documented that as we age there is precipitous drop in GSH levels. Lower Glutathione levels are implicated in many diseases associated with aging; Cataracts, Alzheimer's disease, Parkinson's, arteriosclerosis, as well as others. Journal of Clinical Epidemiology 47: 1021-28 1994

Strong muscular activity generates oxyradicals leading to muscle fatigue and poorer performance. GSH neutralizes these radicals. Whey proteins promotes muscular development. Sports Medicine 21; 213 - 238, 1996. Recent studies indicate that propensities toward many degenerative diseases and aging itself are related to the capacity of the cell to robustly recover from oxidative insult. The capacity of a cell to recover from such insult can be determined by measuring the intracellular stores of Glutathione. (Noelle et al., 1981)

Antioxidant Functions
Antioxidants are well documented to play a vital role in health maintenance and disease prevention. GSH is our cell's own major antioxidant. We should use what is natural. Biochemical Pharmacology 47:2113-2123 1994

Neurological Disease
Low GSH has been demonstrated in nuerodegenerative diseases such as MS (Multiple Sclerosis), ALS (Lou Gehrig's Disease), Alzheimer's, and Parkinson's, among others. The Lancel 344: 796-798 1994

Toxins, Pollution, Radiation
GSH detoxifies many pollutants, carcinogens and poisons, including many in fuel exhaust and cigarette smoke. It retards damage from radiation such as seen with loss of the ozone. Annual Review of Biochemistry 52: 711-780 1983. The liver is the main detoxification organ of the body. In the liver we find very high concentrations of GSH, as it is a major factor in numerous biochemical detoxification pathways. Numerous studies have demonstrated that patients with compromised liver function due to alcohol abuse have significant reduction of GSH in the liver. (Lamest, 1995)

Low Glutathione levels with poor survival in AIDS patients. Much literature has been written demonstrating the role of enhancing GSH levels in AIDS. Proc. National Acad. Science USA 94: 2967-72 1997

1. Biochemical Pharmacology 47:2113-2123 1994
2. Droege W, Holm E. Role of cysteine and glutathione HIV-wasting and other diseases associated with muscle wasting and immunoglobulin function. FASEB J 1997; 11:10771089
3. WHEY PROTEIN REPORT, Current Concepts on Whey Protein Usage, Prepared for The Cleveland Eye Clinic, by: David Marshall, Jr., O.D., Ph.D., Consult

Bovine Serum Albumin, alpha-Lactalbumin and beta-Lactoglobulin

Bovine serum albumin enhances pregastric lipase's, promoting more efficient newborn digestion, further it also binds fatty acids in the body. More essential is that it contains an appreciable amount of cysteine, which is the molecular precursor to glutathione.

Alpha-lactalbumin is the subunit of lactose synthesis the enzyme which catalyzes the addition of galactose to glucose to create lactose*. It is possible this may aid in infant digestion of milk. It also contains cysteine, though not in as great a ratio as bovine serum albumin.

Beta-lactoglobulin is involved with the transfer of passive immunity and the binding of retinol and fatty acids. This binding allows for the efficient uptake of fats by the cells.

The presence of beta-lactoglobulin and alpha-lactalbumin protein in milk is a major cause for allergic reaction in humans. Subsequently, those with true milk allergies to milk protein should not ingest these milk proteins and should caution their use in any form. Lactose intolerance is not a factor in this allergic response. Typically lactose intolerance presents itself as diarrhea from the excess consumption of lactose (this can vary from individual to individual). Healthy Planet Vitamins purest proteins contain low levels (0.3g per 5g serving) of lactose and this is well below the tolerance level for most people.


Whey Protein Facts and Applications

Dr. Lawrence Sosna

The word Protein means “first substance”. Our first protein food was found in our mother’s milk. Milk is the only food designed specifically to optimally sustain the life of a mammal. In fact, the root word for nutrition means to suckle.  As a species, we would not have survived if not for the nutrition and protection mother’s milk offers.

Whey is one of the two protein groups found in milk. It is a liquid complex consisting of a wide range of proteins. The other protein group is casein, which curds are made from and then processed into cheese.

Whey is an original complete protein food and is considered number one for building and regenerating our bodies and maintaining a strong immune system.  Our entire metabolic process relies on the intake of complete protein.  We cycle proteins into amino acids constantly.

Hippocrates, the Greek physician of the 5th century B.C., the “father of medicine”, stated that the body has an inner adaptive or healing power. To strengthen this healing power, he prescribed serum (liquid whey) to his patients. It was true non-denatured, native whey. It provided full biological activity and numerous health benefits. All commercial whey proteins available now are derived from extensively processed milk and incomparable to the vitality in that 2500 year-old prescription.

It is appropriate to review some important definitions of terms used:

Native Protein: The naturally occurring conformation of a protein. Unaltered by heat, chemicals, enzyme action or processing. (Native is the same structure and proportion as in the original substance.)

Denatured: To cause the tertiary structure of (a protein) to unfold, as with heat, alkali, or acid, so that some of its original properties, especially its biological activity, are diminished or eliminated. (It means damaged.)

Undenatured: To undamage. (A term that is used without discretion in the industry and is misleading. It is not possible for a protein to be undenatured.)

Non-denatured: The same structure and proportion as in the original substance with full biological activity. (Never damaged.)

Presently, the various commercial methods of processing whey do not improve or even maintain the fragile immune modulating and regenerative components or the biological activity that was originally in the milk. They all originate from the manufacturing of cheese and are by-products.

There are three commercial production methods, which comprise the majority of available whey proteins. They are isolates (the most popular), ion-exchange and hydrolyzed forms. They are all ultrafiltered, cross-flow filtered or microfiltered via elaborate patented methods developed by large dairies. The milk used in these three methods undergoes major processing that involves high heat (163 degrees F) and drastic acidification of the whey to produce curds for manufacturing cheese. These steps denature (damage) the proteins. What is then required is extensive filtration to remove the many denatured proteins in order to produce the highest percentage of protein. Unfortunately the fragile vital protein components, which determine the biological activity of the protein, are not retained. The terms undenatured and cold-process are prevalent with these commercial products, but once a protein is denatured it is not possible to undenature it. 

The key point in regard to the quality and effectiveness of whey is that the full range of biological activity and proportion of the protein components be preserved in their original native form as nature provided. Only whey that is not involved in cheese manufacture can achieve that goal. Additionally, the health of the milking cows and quality of the milk is the foundation of this type of product.

Non-denatured whey protein has the highest biological value of any protein. It is a complete protein, unlike soy, and provides all the essential amino acids in the correct balance. The five major active proteins of whey are lactoferrin, immunoglobulins, bovine serum albumin, alpha-lactalbumin and beta-lactoglobulin. There are many whey products available; therefore it is highly advisable to have in writing from the manufacturer, the treatment of the cows, the entire processing the milk undergoes and if cheese is part of the original production. Also request a written laboratory analysis that lists the percentage values for each individual protein. An analysis that groups two or more proteins together with a percentage number is very questionable and worthless to a discriminating professional or consumer.  

Covalent Bonded Cysteine (the non-denatured form), is the critical amino acid required for the all-important intracellular production of the antioxidant glutathione (GSH). Glutathione is our body’s master antioxidant and is responsible for numerous defense and repair functions and is an effective antiaging substance. Glutathione is best utilized when we produce it internally. Cysteine is very scarce in our modern diet and therefore glutathione production is limited and deficiency is prevalent. If cysteine undergoes any heating or processing, as all commercial whey products do, it is denatured and converted to cystine. Covalent-bonded cysteine, active peptides, anabolic growth factors and enzymes are also present in non-denatured native whey, as there is no processing to denature them.

The public is now becoming more aware of the value of quality protein and is choosing whey protein for many good reasons. Not only does non-denatured whey have a wide range of immune-enhancing properties, it also has the ability to act as an antioxidant, antihypertensive, antitumor, antiviral and antibacterial. A number of clinical trials have successfully been performed using whey as an antimicrobial agent and in the treatment of cancer, HIV, hepatitis B & C, cardiovascular disease and osteoporosis. It has a major role in red blood cell production, support in chemotherapy treatment, safe binding and detoxification of heavy metals, wound healing, growth of new muscle, weight regulation and the support of numerous immune functions. It is used by populations that have Chronic Fatigue Syndrome (CFS), Fibromyalgia, Hepatitis, Cancer, HIV/AIDS, Respiratory disease, cognitive disorder from nutritional compromise and for any sports performance improvement.

Dr. Lawrence Sosna

Dr. Lawrence Sosna Graduated first in his class from the Fairfield College of Myopractics and Naturopathic Medicine. He is a N.D. and has a PhD in Myology with an emphasis in Orthomolecular Biochemistry. He strictly practices Integrative Medicine - his research field being cellular regeneration, Anti-Aging and bio-identical comprehensive hormone replacement therapy. Dr. Sosna lectures on these topics at symposiums all over the world.  Recently Dr. Sosna has been appointed Dean of the College of Naturopathic Medicine in Encinitas California.


Whey Protein Facts and Applications


Bonang G, Monintja HE, Sujudi, van der Waaij D. Influence of breastmilk on the development of resistance to intestinal colonization in infants born at the Atma Jaya Hospital, Jakarta. Scand J Infect Dis 2000;32:189-196.

Bounous G. Whey Protein concentrate and glutathione modulation in cancer treatment, Anticancer Res. 2000;20:4785-92

Bounous G, Kongshavn PA. Influence of dietary proteins on the immune system of mice. J Nutr 1982;112:1747-1755.

Bounous G, Gervais F, Amer V, et al. The influence of dietary whey protein on tissue glutathione and the diseases of aging. Clin Invest Med 1989;12:343-349.

Bowen J, Noakes M, Clifton P. Whey Protein and body fat loss. Asia Pac J Clinical Nut. 2003; 12:S9

Crinnion WJ. Environmental medicine, part 2 – health effects of and protection from ubiquitous airborne solvent exposure. Altern Med Rev 2000;5:133-143.

Guimont C, Marchall E, Girardet JM, Linden G. Biologically active factors in bovine milk and dairy byproducts: influence on cell culture. Crit Rev Food Sci Nutr 1997;37:393-410.

Ha E, Zemel MB. Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people (review). J Nutr Biochem 2003;14:251-258.

Hakkak R, Korourian S, Ronis MJ, et al. Dietary whey protein protects against azoxymethane-induced colon tumors in male rats. Cancer Epidemiol Biomarkers Prev 2001;10:555-558.

Jones EM, Smart A, Bloomberg G, et al. Lactoferricin, a new antimicrobial peptide. J Appl Bacteriol 1994;77:208-214.

Kawase M, Hashimoto H, Hosoda M, et al. Effect of administration of fermented milk containing whey protein concentrate to rats and healthy men on serum lipids and blood pressure. J Dairy Sci 2000;83:255-263.

Kennedy RS, Konok GP, Bounous G, et al. The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: a phase I-II clinical trial study. Anticancer Res 1995;15:2643-2649.

Kimball SR, Jefferson LS. Control of protein synthesis by amino acid availability. Curr Opin Clin Nutr Metab Care 2002;5:63-67.

Lands LC, Grey VL, Smountas AA. Effect of supplementation with a cysteine donor on muscular performance. J Appl Physiol 1999;87:1381-1385.

Laursen I, Briand P, Lykkesfeldt AE. Serum albumin as a modulator on growth of the human breast cancer cell line MCF-7. Anticancer Res 1990;10:343-351.

Levay PF, Viljoen M. Lactoferrin: a general review. Haematologica 1995;80:252-267.

Markus CR, Olivier B, de Haan EH. Whey protein rich in alpha-lactalbumin increases the ratio of plasma tryptophan to the sum of the other large neutral amino acids and improves cognitive performance in stress-vulnerable subjects. Am J Clin Nutr 2002;75:1051-1056.

Marshall David Jr., O.D., Ph.D. WHEY PROTEIN REPORT - Review of Various Whey Protein. Current Concepts on Whey Protein Usage.

Micke P, Beeh KM, Buhl R. Effects of longterm supplementation with whey proteins on plasma glutathione levels of HIV-infected patients. Eur J Nutr 2002;41:12-18.

Sawatzki G, Rich IN. Lactoferrin stimulates colony stimulating factor production in vitro and in vivo. Blood Cells 1989;15:371-385.

Smithers GW, McIntosh GH, Regester GO, et al. Anti-cancer effects of dietary whey proteins. Proceedings of the Second International Whey Conference 1998;9804:306-309.

Shah NP. Effects of milk-derived bioactives: an overview. Br J Nutr 2000;84:S3-S10. Sundberg J, Ersson B, Lonnerdal B, Oskarsson A. Protein binding of mercury in milk and plasma from mice and man – a comparison between methylmercury and inorganic mercury. Toxicology 1999;137:169-184.

Takada Y, Aoe S, Kumegawa M. Whey protein stimulated the proliferation and differentiation of osteoblastic MC3T3-E1 cells. Biochem Biophys Res Commun 1996;223:445-449.

Tsuda H, Sekine K, Ushida Y, et al. Milk and dairy products in cancer prevention: focus on bovine lactoferrin. Mutat Res 2000;462:227-233.

Watanabe A, Okada K, Shimizu Y, et al. Nutritional therapy of chronic hepatitis by whey protein (non-heated). J Med 2000;31:283-302.

Walzem RL, Dillard CJ, German JB. Whey components: millennia of evolution create functionalities for mammalian nutrition: what we know and what we may be overlooking. Crit Rev Food Sci Nutr 2002;42:353-375.

Yamamura J, Aoe S, Toba Y, et al. Milk basic protein (MBP) increases radial bone mineral density in healthy adult women. Biosci Biotechnol Biochem 2002;66:702-704.

Proteins Duke it Out for Prominence,
but Only One is a True Champion

Carlon M. Colker, M.D.

Although debated for years, it is now not merely a widely held belief, but an accepted fact, that athletes and people who exercise need more protein than sedentary non-exercising individuals.1-9 But as protein has gained in popularity and finally assumed its rightful place as king of the macronutrients, a new war has begun. The battlefield has been drawn, pitting all available sources of protein against each other in an all-out brawl to see which rules. In the words of Apollo Creed- when he was set to face the Italian Stallion- "Sounds like a damn monster movie!" Of course, if you've been paying attention to the media, you know that two top contenders have emerged.

Hold the fort down fight fans, and let's get ready to rumble! In the blue corner, a lower quality protein weighing in without all the essential amino acids, a debatable cardio-protective effect, and a known and worrisome phytoestrogen content soy protein. In the red corner, the highest quality and biologics value protein, weighing in with all the essential amino acids, immune enhancing powers, and offering greater cancer protection than soy - whey protein!

Sounds like a mismatch to me. Of all the protein sources out there, you might wonder why these two have emerged as top dogs. The answer is that whey protein is in contention as a result of a wellspring of supporting research and scientific fact. Soy protein, on the other hand, has emerged for honors simply because of clever exaggerations of flimsy studies, as well as misleading propaganda driven by a powerful and profit oriented soy lobby.

Sorry soy enthusiasts, if I've touched a sore spot. But let's examine this issue further and include the important basic differences, as well as some of the latest research on both these proteins.

The Big Lie
First of all, I'm tired of hearing all this garbage about soy being a complete protein (meaning it contains all the essential amino acids our bodies can't synthesize from other sources and must instead directly consume). Don't let anyone shove this lie down your throat. Soy protein is not a complete protein because it lacks the amino acid methionine. This is a non-debatable scientific fact.

Whey protein, on the other hand, lacks no essential amino acids. As a result, it has a much higher biological value in terms of similarity to our own human protein. Whey protein beats soy protein hands down in this category simply because whey protein needs no fortification or additive to make it complete. It is complete in its natural form.

Perhaps the greatest coup for soy fans of late was approval by the FDA for soy-containing products to be listed as able to reduce the risk of heart disease This government seal of approval was not only premature, but also potentially dangerous. There was, and still is, no solid scientific research to back such cavalier support by our government. I wonder how a government steeped in the practice of forcing products to be thoroughly researched and tested before claims can be made, would do something so reckless.

The fact is, soy has no more impressive research to support such broad-based government support than that which supports whey protein in the area of heart health. The research supporting soy as cardio-protective is almost completely epidemiological and observational across broad spectrums of the population. In fact, as far as whey protein is concerned, nearly a decade ago the Chinese demonstrated the cholesterol and plasma lipid lowering ability of whey protein.10 But this, along with piles of subsequent research, hasn't motivated the government to give whey protein the same whorish kiss it gave soy.

Much Ado About Estrogen
I think what's really going on starts with the soy lobbyists. Soy is big business. Nearly a million metric tons have come into this country this past year alone; nearly $500 million worth of soy products moved off supermarket shelves just last year.11 When big bucks are on the line, lobbyists find the motivation to aggressively seduce government.

A lot of support for soy being heart healthy stems from soy enthusiasts focusing on the estrogenic effect of soy. Soy contains genistein and other phytoestrogens that are hormonally akin to estrogen. Unfortunately, it now appears these folks have jumped the gun. A landmark study in the Journal of the American Medical Association looked at estrogen therapy and the prevention of heart disease.

The study showed that over four years, estrogen treatment did not reduce the rate of heart disease in postmenopausal women. In fact, it increased the rate of blood clots and gallbladder disease! The conclusion of this comprehensive study of nearly 3,000 subjects sent a clear message to physicians that, while it might help bone density and lessen the chance of hip fractures, estrogen therapy does not protect the heart. Thus, it should not be given for preventing heart disease. "Based on the finding of no overall cardiovascular benefit and a pattern of early increase in risk of CHD (coronary heart disease) events, we do not recommend starting this treatment for the purpose of secondary prevention of CHD."12

Thus, those taking soy as an estrogen analog for protection against heart disease have been woefully misled by the propaganda. In fact, as the research clearly shows, the road of estrogenic substances is filled with perils., Why the soy supporters and the FDA have ignored this, is beyond, my comprehension. I should highlight here that, unlike soy protein, whey protein has no phytoestrogen content. And, while the exact mechanism remains unclear, the cardioprotective effect, if any, probably has more to do with a powerful antioxidant effect that benefits the entire body, not just the heart.

There are other problems with exposure to estrogens and estrogen-like substances, namely cancer. Somehow soy got labeled a cancer preventive! The absurdity of this flawed logic makes me laugh; the potential health ramifications of the misinformation make me cry.

Receptor Site Skirmish
The theory behind soy as a cancer preventive stems from the fact that the phytoestrogens in soy protein, although estrogen-like in function, are weaker receptor stimulators than the estrogens in our bodies. When this weaker estrogen is put in the body, it competes with the body's own estrogens for receptor sites. A temporary "blocking" effect is exerted because these estrogen-like compounds don't stimulate the receptor to the same degree as actual estrogens. This is the mechanism of action of tamoxifin, a chemotherapy agent many soy supporters say soy protein is akin to.

The problem with this theory: While an estrogen-like substance might have a weaker stimulatory property on one area of receptors in the body, it may be stimulatory to the same degree as true estrogen at other receptor sites. It's for this reason drugs with more estrogen site specificity are currently being developed. New drugs like raloxifene appear to have estrogen site selectivity so that, for the postmenopausal female, the risk of osteoporosis is reduced without stimulating uterine or breast cancer.13

So, while phytoestrogens in soy might be weaker estrogens at some sites in the body and thus help prevent cancer spurred by the body's own unopposed estrogens, it has no receptor site specificity, and thus may actually stimulate cancer, in other areas of the body.14

In fact, in recent discussions with prominent cancer specialists and colleagues at the world renowned Memorial Sloan Kettering Cancer Center in New York, the subject of soy protein came up. All three specialists I spoke with are telling successfully treated breast cancer survivors to avoid soy. Of even greater interest was that they maintained this recommendation even for those individuals whose cancer was deemed "non-estrogen dependent" (i.e., estrogen receptor negative). They said they did this "just to be on the safe side."

Russian Roulette?
But, thankfully, the public is getting hip. In a recent New York Times article, prominent physician researchers called our attention to the potential perils of soy. Dr. Margo Woods at tufts University School of Medicine, Dr. Gregory Burke at Wake Forest University School of Medicine, Dr. William Helferich at the University of Illinois, and even the FDA's own research biologist at the National Center for toxicological Research, have all voiced very serious concerns."

My recommendation would be to examine your family history carefully. If you have a history of cancer (especially breast), consider soy a danger.
But if it's cancer prevention you're interested in, without playing Russian roulette with the phytoestrogens found in soy, take a good look at whey protein. More than a decade ago, whey protein demonstrated an ability to prevent cancer and tumor growth.15
The current thought is, in much the way whey protein may be cardio-protective, the key mechanism of action has to do with whey's unique ability to bolster the immune system by increasing intracellular antioxidant power.

We have all heard of vitamins E and C and their antioxidant ability in the bloodstream. But, a far more powerful and target-specific antioxidant exists within each living cell called gamma-L-glutamyl-L-cysteinyl-glycine, more easily referred to as GSH (Glutathione). This powerful antioxidant exerts its action within the cell. In fact, it cannot only be synthesized inside the cell from smaller molecules since there is no efficient transport mechanism to get GSH from the blood stream into the cells.

The key building block for GSH is an amino acid called cysteine. When two molecules of cysteine are coupled and then linked by a disulfide bond, the result is a molecule called cystine. This cystine molecule is not only stable, but travels easily through the body and into each living cell. Once in the cell, it's broken down into cysteine molecules; and used to form GSH.

Because of whey protein's unmatched biological value, bioavailability, impressive solubility, level of absorption, and high percentage content of cystine residues and branch chain amino acids (23 percent), it's the superior form of protein supplementation for athletes.16 Though moderate exercise has been shown to improve immunity, intense exercise has been shown to reduce GSH levels, which are associated with immunosuppression.17 This negative effect on immunity is directly related to the intensity and duration of the physical activity and immune status of the athlete. Over the past decade it has been shown that whey protein possesses immune enhancing properties that can help the athlete recover and avoid over training syndrome.18

Unlike soy protein, which is profoundly deficient in these and other sulfur-containing amino acids whey protein (in particular, the concentrate form) contains an abundance of highly biologically active cystine residues, thus making it a powerful immuno-modulator against cancer, toxins, infections, or any other bodily insult.19

Staggering News
In support of the notion of whey being protective, against cancer, a recent study published by the American Association for Cancer Research compared whey Protein to soy protein and casein ( a low order milk protein). The article concluded that "Whey appears to be at least twice as effective as soy in reducing both tumor incidence and multiplicity."20 This staggering news has profound ramifications with respect to choosing between soy protein and whey protein.

Furthermore, the same "cysteine donor" effect unique to whey and not found in soy, that seems to be at work in preventing cancer, has recently been shown to enhance muscular performance and decrease muscular fatigue. Another recent study concluded that prolonged supplementation with a product designed to augment antioxidant defenses resulted in improved volitional performance."21 Remember, this characteristic is unique to whey and something soy simply cannot achieve because it is not a cysteine donor.

Going back to the issue of soy containing phytoestrogens, the problem may be worse for men than for women.
The research indicates that these phytoestrogens are not as weak and harmless as soy enthusiasts would lead you to believe. In fact, when genistein (the main phytoestrogen in soy) Was given to mice in doses similar to those contained in an average soy-based diet, in only nine days testosterone concentration was dramatically reduced. The reduction seemed to stem from a decrease in production of luteinizing hormone, secreted by the anterior pituitary gland.22 In fact, several other animal studies clearly indicate the rather frightening feminizing effect of unopposed estrogen stimulation in the form of dietary phytoestrogens.23,24

My own fight card says soy loses yet another round. Stick with whey, unless of course you want to get in touch with your feminine side.
Moreover, another recent, study by Dr. Stephen Liu of UCLA Medical Center, demonstrated the influence of estrogen on weakening ligaments and thus increasing the probability of injury. This would explain why women are up to six times as likely as men to suffer an anterior cruciate ligament tear.25 Although this research is somewhat controversial and preliminary, it warrants careful examination. As with the concerns over soy protein negatively influencing thyroid function in children, don't discard these possible early indicators of what could become a serious health issue as the soy juggernaut rolls on unopposed.
As we near the end of the final round, know that the research continues to mount supporting whey as the protein of choice and, unless used carefully only in select cases as a medicinal food, soy is far inferior and dangerously problematic. In this head-to-head battle, soy protein is simply outclassed by whey. But since the Don Kings of the soy industry are showing no signs of letting up on the pro-soy hype, something tells me this mismatch is destined for a rematch.


1. Brouns F. et al. Metabolic changes induced by sustained exhaustive cycling and diet manipulation. lnt J Sports Med. 10(Suppl.1):S49-S62,1989.
2. Dolny D.G. et al. Effect of ambient temperature on protein utilization during prolonged exercise. J Appl Physiol.64:550-555, 1988.
3. Lemon P. Effects of exercise on dietary protein requirements. Int ,J Sports Nutr. 8:426-447 1988
4. Lemon P. Do athletes need more protein and amino acids? lnt J Sport Ntrtr. 5(Suppl):S39-S61, 1995
5. Lemon P. Effects of exercise on protein and amino acid metabolism. Mod Sci Sports Exerc. 13:141-149,1961.
6. Lemon P. et al. Protein requirements and muscle mass/strength changes during intensive training novice bodybuilders. J Appl Physiol. 73:767-775, 1992.
7. Meredith C.N. et al. Dietery protein requirements and protein metabolism in endurance-trained men. J Appl Physiol. 66:2850-2856, 1989.
8. Tamopoisky M.A. et al. Evaluation of protein requirements strength trained athletes. J Appl Physiol. 73:1986-1995, 1992.
9. Tarnopolsky MA at al. Influence of protein Intake and training status on nitrogen balance and lean body mass. J Appl Physiol. 64:187-193,1988.
10. Zhang X. et al. Whey proteins, effect on plasma and triacylglyerols. Brit J Nutr. 1993.
11. Burros M. Doubts cloud rosy news on soy. The Science Times The New York Times Jan. 26, 2000.
12. Hulley S. et al. Randomized trial of estrogen plus progestin for secondary prevention of coronary heart disease in postmenopausal women. JAMA. 1998;280:605-612.
13. Cummings S.R. et al. The effect of raloxifene on risk of breast, cancer in postmenopausal women. JAMA. 1999;281:2189-2197.
14. Willet W. at al. Postmenopausal estrogens- Opposed, unopposed, or none of the above. JAMA. 2000;283:534-535.
15. Bounos G. Whey protein and cancer. Clin Invest Med..1998.
16. Satterman W. Whey protein for athletes. Dtsh Milchwirsch. 1986; 37(33):1010- 1012.
17. Nowsholme EA. Biochemical mechanisms to explain immunosuppression in well-trained and overtrained athletes. Int J Sports Med 1994;15(3):sl42-47.
18. Colker C., Kalman D., Brink W., Antonio J. Immune status of elite athletes, Role of whey protein concentrate. Med Sci Sports Exerc 1998;30(5):a95.
19. Bounos G. The story behind a health-promoting product-patented milk serum (whey) protein concentrate. lmmunotec Clinical Foundations. 1998.
20. Hakkak R. et al. Diets containing whey proteins Or soy protein isolate protect against 7,12-dimethylbenz(a)anthracene-induced mammary tumors in female rats. Canc Epid Bio Prev. 2000;9:113-117.
21. Lands LC. Effect of supplementation with a cysteine donor on muscular performance. J Appl Physiol. 1999;87(4):1381-1385.
22. Strauss E. et al. Genistein exerts estrogen-like effects in the male mouse reproductive tract. Mol Cell Endocrinol. 1988;25.144(1-2):83-93.
23. Casanova M. et al. Developmental effects of dietary phytoestrogens in Sprague-Dawley rats and interactions of genistsin and diadzein with rat estrogen receptors alpha and beta in vitro. Toxicol Sci. 1999;51(2):236-244.
24. Kumi-Diaka J. et al. Cytotoxic potential of the phytochemical genistein isoflavone and certain environmental chemical compounds on testicular cells. Biol Cell. 1999;91(7)-515-523.
25. Female hormones blamed for knee injury; The NewYork Pbst, Jan. 29, 2000.

Copyright ©  2008 Healthy Planet Vitamins LLC, Website Developed by WiseWorldMedia