Take away the water and about 75 percent of your weight is protein. This chemical family is found throughout the body. it's in muscle, bone, skin, hair, and virtually every other body part or tissue. It makes up the enzymes that power many chemical reactions and the hemoglobin that carries oxygen in your blood. At least 10,000 different proteins make you what you are and keep you that way.
Twenty or so basic building blocks, called amino acids, provide the raw material for all proteins. Following genetic instructions, the body strings together amino acids. Some genes call for short chains, others are blueprints for long chains that fold, origami-like, into intricate, three-dimensional structures.
Because the body doesn't store amino acids, as it does fats or carbohydrates, it needs a daily supply of amino acids to make new protein.
Many people think of nuts as just another junk food snack. In reality, nuts are excellent sources of protein and other healthful nutrients.
One surprising finding from nutrition research is that people who regularly eat nuts are less likely to have heart attacks or die from heart disease than those who rarely eat them. Several of the largest cohort studies, including the Adventist Study, the Iowa Women's Health Study, the Nurses' Health Study, and the Physicians' Health Study have shown a consistent 30 percent to 50 percent lower risk of myocardial infarction, sudden cardiac death, or cardiovascular disease associated with eating nuts several times a week. In fact, the FDA now allows some nuts and foods made with them to carry this claim: "Eating a diet that includes one ounce of nuts daily can reduce your risk of heart disease."
There are several ways that nuts could have such an effect. The unsaturated fats they contain help lower LDL (bad) cholesterol and raise HDL (good) cholesterol. One group of unsaturated fat found in walnuts, the omega-3 fatty acids, appears to prevent the development of erratic heart rhythms. Omega-3 fatty acids (which are also found in fatty fish such as salmon and bluefish) may also prevent blood clots, much as aspirin does. Nuts are rich in arginine, an amino acid needed to make a molecule called nitric oxide that relaxes constricted blood vessels and eases blood flow. They also contain vitamin E, folic acid, potassium, fiber, and other healthful nutrients.
Eating nuts won't do much good if you gobble them in addition to your usual snacks and meals. At 185 calories per ounce, a handful of walnuts a day could add 10 pounds or more in a year if you don't cut back on something else. This weight gain would tip the scales toward heart disease, not away from it. Instead, eat nuts instead of chips or other, less healthy snacks. Or try using them instead of meat in main dishes, or as a healthful crunch in salads
Protein And Chronic Disease
The most solid connection between proteins and health has to do with allergies. Proteins in food and the environment are responsible for these overreactions of the immune system to what should be harmless proteins. Beyond that, relatively little evidence has been gathered regarding the effect of protein on the development of chronic diseases.
|Foods||Serving||Weight in grams||Protein grams||% Daily Value|
|Hamburger, extra lean||6 ounces||170||48.6||97|
|Chicken, roasted||6 ounces||170||42.5||85|
|Tuna, water packed||6 ounces||170||40.1||80|
|Beefsteak, broiled||6 ounces||170||38.6||77|
|Cottage cheese||1 cup||225||28.1||56|
|Cheese pizza||2 slices||128||15.4||31|
|Yogurt, low fat||8 ounces||227||11.9||24|
|Lentils, cooked||1/2 cup||99||9||18|
|Skim milk||1 cup||245||8.4||17|
|Split peas, cooked||1/2 cup||98||8.1||16|
|Whole milk||1 cup||244||8||16|
|Lentil soup||1 cup||242||7.8||16|
|Kidney beans, cooked||1/2 cup||87||7.6||15|
|Cheddar cheese||1 ounce||28||7.1||14|
|Macaroni, cooked||1 cup||140||6.8||14|
|Whole wheat bread||2 slices||56||5.4||11|
|White bread||2 slices||60||4.9||10|
|Rice, cooked||1 cup||158||4.3||9|
|Broccoli, cooked||5 inch piece||140||4.2||8|
|Baked potato||1 Medium||156||3||6|
|Corn, cooked||1 ear||77||2.6||5|
Nutritive Value Of Foods, USDA
PROTIEN REQUIRED TO MAINTAIN LEAN MUSCLE
Lean Body Weight Method
Step #1 Calculate your lean body weight (Example 200# and 20% Body Fat) = 100% - 20% = 80%
Step #2 Multiply (Example 200 X .80 ) = 160# lean body weight
Step #3 Multiply lean body weight times 1 (Grams Of Protein Needed Per Day) = 160 gr.
Step #4 Subtract breakfast protein (Example 3 oz. steak and 2 eggs) = est. -32 gr.
Step #5 Subtract lunch protein (Example 6 oz. chicken and 2 bread) = est. -48 gr.
Step #6 Subtract dinner protein (Example 6 oz. fish and 2 vegetables) = est. -48 gr.
Step #7 Total grams of protein supplement needed to MAINTAIN muscle mass and weight = est. 32 gr.
Step #8 Total scoops of protein needed (32 divided by 16 grams of protein per scoop) = est. 2 Scoops
(Supplement Protein Should Be Taken After A Workout And Prior To 8:00 PM)
Total Body Weight Method (Example 200#)
Step #1 Multiply total body weight times .8 = grams of protein needed per day = 160 gr.
Step #2 Subtract breakfast protein (Example 3 oz. steak and 2 eggs) = est. -32 gr.
Step #3 Subtract lunch protein (Example 6 oz. chicken and 2 bread) = est. -48 gr.
Step #4 Subtract dinner protein (Example 6 oz. steak and 2 vegetables) = est. -48 gr.
Step #5 Total grams of protein supplement needed to MAINTAIN muscle mass and weight = 32 gr.
Step #6 Total scoops of protein needed (32 divided by 16 grams of protein per scoop) = est. 2 Scoops
(Supplement Protein Should Be Taken After A Workout And Prior To 8:00 PM)
Material originally published at www.jonbarron.org.
Copyright © 1999-2011. Baseline of Health® Foundation
Used by permission of the Baseline of Health® Foundation.
All rights reserved worldwide.
By: Jon Barron
Protein, Part 1
Over the years, I've talked extensively about carbohydrates, fats, fiber, vitamins, minerals, and antioxidants, but not so much about protein. Then again, what's to say about protein? Protein is protein, right? it's the stuff in meat, chicken, fish, and soy. There may be different sources, but it's all the same, isn't it? it's not like there are different kinds of protein. You can't break dietary protein into subgroups like you can with fat -- categorizing it as saturated, unsaturated, and trans fats. Or can you? As it turns out, protein is not so simple, and there are a number of questions that need to be addressed when you're thinking about what protein to eat such as bioavailability, speed of uptake, the size of the protein molecule, allergies, etc. And since I'm currently involved in a project to develop the next generation of hypoallergenic protein, now seemed as good a time as any to address the issue. Let's begin by covering the basics and then spiraling out in ever expanding detail.
What Is Protein And How Does It Relate To Diet And Health And Diet?
The simplest, least useful, definition is that proteins are long chain molecules made up of amino acids joined by peptide bonds. Next to water, protein is the most plentiful substance in your body and is the principal constituent of the protoplasm in every cell of your body. That said, there is not just one kind of protein, but many kinds in the human body, each with a different function. For example, different proteins can:
- Provide structure, as found in ligaments, fingernails, and hair
- Aid in digestion in the form of digestive enzymes
- Play a role in immunity in the form of immunoglobulins
- Aid in movement in the form of muscles
- Tell your body what to do and when as seen in peptide hormones
- Transport oxygen as hemoglobin
- And even play a role in our ability to see. The lens of the eye is pure crystallin protein.
Interestingly enough, your body does not actually utilize protein directly when you eat it. When you consume protein, for the most part, the body breaks it down into its constituent amino acids, absorbs those amino acids through the intestinal tract, and then using genetic instructions encoded in your body, reassembles them into the proteins it needs to perform all its functions. For example, it takes dairy protein you eat, breaks it down in the digestive tract into its constituent amino acids, absorbs those amino acids, and then reassembles them into muscle protein to help you become Arnold Schwarzenegger. Thus, milk protein from Elsie the Cow becomes the Governor of California. Whenever the body assembles a protein from amino acids, when it builds muscle for example, it needs a variety of amino acids to complete the process. Some of these amino acids may be produced in the body itself. Others may come from dietary sources. But nine amino acids can only come from dietary sources because your body cannot produce them no matter what you eat. These nine are considered essential, not because they're more important, but again because your body cannot manufacture them and therefore they must be part of your diet on a regular basis. These include:
- Histidine (your body can manufacture histidine, but usually not in sufficient amounts)
If your diet is chronically deficient in any one of the essential amino acids, the building of protein in the body stops, which brings us to a key point. Your ability to utilize protein is profoundly affected by the " limiting amino acid" in your diet -- kind of a "you're only as strong as your weakest link sort of thing." For example, if you are vegetarian and rely on rice for your protein, rice tends to be low in lysine. Over time, the lack of lysine in your diet may become a limiting factor in the ability of your body to assemble proteins. Simply adding legumes, which are high in lysine, to the diet corrects the problem and allows your body to build all of the proteins that it needs. It is a good idea, therefore, to mix your protein sources so that deficiencies in any one source are corrected by another. In addition, this limits the loss of nitrogen in the liver where amino acids are broken down, thereby releasing ammonia and causing an increase in the production of uric acid. Bottom line: getting a good mix of amino acids in your protein sources increases your overall net protein utilization and reduces the chances of gout.
To summarize everything that we've covered so far, Let's just say that protein, as a category, is one of the essential nutrients along with carbohydrates, fats, vitamins, minerals, oxygen and water. In fact, the word protein comes from the Greek word "prota", meaning "of primary importance." Protein has a critical physiological function. It is primarily used in the body to build, maintain, and repair body tissues. In some cases, if protein intake is greater than that required by the body to perform its primary function, the excess protein may be converted to energy for immediate use (as happens with bodybuilders and performance athletes) or it will be stored in the body as fat (as happens for the rest of us). Note: protein will only be used by the body as an energy source after other energy sources (i.e., carbohydrates and fats) are exhausted or unavailable.
And that concludes Protein 101. Now Let's move on to the more interesting stuff.
Structure of protein and how it's digested and utilized
Protein bioavailability is not just a function of the amino acids that are present. it's also dictated by the structure of the protein. Some proteins are more amenable to being broken down (digested) than others. For the purposes of this newsletter, we don't really have to plumb the depths of biochemistry, or the nature of the peptide bonds that hold proteins together. However, it is necessary to discuss briefly how proteins are assembled from amino acids and the various shapes those proteins take.
There are some 20 different amino acids which are commonly identified. Each and every protein is made from these 20 amino acids put together in varying order and in varying amounts and combinations, thus providing the possibility of almost limitless combinations. That said, most proteins are large molecules that may contain several hundred to many thousand amino acids arranged in branches and chains .
The assembly of amino acids into proteins is actually determined and directed by information encoded in your genes. Each protein has its own unique amino acid sequence as specified by the gene encoding that particular protein. Protein synthesis takes place inside cellular cytoplasm and can actually reach a rate as high as the joining of up to 20 amino acids per second in a given cell. In fact, the assembly of amino acids is responsible for more than just the creation of protein. It is also responsible for the creation of peptides and polypeptides, which can be thought of as "short" or "incomplete" proteins. It should not be surprising then that the definitions of proteins, polypeptides, and peptides somewhat overlap. The protein designation, however, is generally used to refer to longer, complete biological molecules in a stable structure.
The size of a synthesized protein can be measured by the number of amino acids it contains and by its total molecular mass. Some proteins may contain just a few hundred amino acids strung together, but the largest can contain close to 30,000 amino acids all chained together.
So how does a protein composed of a chain of 27,000 amino acids achieve stability? And the answer is through structure. These long chains fold in on themselves to form stable structures.
Most proteins fold into unique 3-dimensional structures. The shape into which a protein naturally folds is known as its native state -- although proteins may shift between several related structures during the course of performing their biological functions.
There are many reasons biochemists try to determine the various structures of any given protein. Most notably, those structures give clues as to the function of the protein in the human body. But for our purposes, there's one primary reason for being aware of protein structure. Protein structure plays a major role in determining how readily it can be broken down into its constituent amino acids during the digestive process. In other words, it plays a major role in determining protein bioavailability its propensity to stimulate allergic responses.
How What You Eat With Protein Affects Your Health
When found in nature, protein never comes by itself. Whether from animal or vegetable sources, protein comes in the presence of various fats and carbohydrates. In most cases, their presence is a non issue. But in a small number of cases, these "extras" play a major factor in determining the digestibility of the protein. For example, some accompanying nutrients can inhibit proteolytic enzymes that would normally break down the protein, or can suppress the release of stomach acid necessary for the digestion of the protein, or simply cover the protein so that enzymes and stomach acid cannot reach it. For example, studies have shown that eating fruit pectin at the same time you eat protein may cover the protein with a hydrogel, which prevents the stomach enzyme pepsin from reaching the protein, thus inhibiting digestion of the protein.
This is not true for all proteins, and requires high pectin fruit to be an issue, but it certainly calls to mind the old food combining axiom not to eat proteins with carbohydrates. Interestingly enough, although such studies support the axiom, they do not necessarily support the theory behind it that the problem results from carbohydrates suppressing the release of gastric juices.
Determining Protein Bioavailability To Optimize Nutrition
Protein bioavailability is the sum total of the three factors we mentioned above:
- The mix of amino acids in the protein -- or in the combination of proteins eaten during the day. Remember, the shortage of an essential amino acid provides a limiting factor on how much of the overall protein can be utilized by the body.
- The structure and size of the protein molecule. The larger and more tightly folded the molecule, the less able the body is to break it down. Large proteins that frequently undergo incomplete digestion include those found in wheat, corn, dairy, and soy. It is not coincidental that these foods are identified by the FDA as being highly allergenic. (We will discuss protein allergies more in our next newsletter.)
- The other foods (or components in the protein source itself) that inhibit the breakdown of the protein.
Protein Utilization Can Be Measured
There are several tests for measuring protein utilization, or bioavailability, although they're a bit like the story of the blind men describing an elephant -- each one gives an incomplete picture. The blind man who feels the trunk says an elephant is like a snake. The one who feels its legs says an elephant is like a tree. The one who feels the ears says an elephant is like a giant fan. And the one who feels its body says an elephant is like a massive wall. Each one provides useful information; but each one also provides an incomplete picture.
The Kjeldahl method is the standard for measuring the total protein concentration in food. It provides the number that you normally see on nutrition labels on the side of food packages. Unfortunately, it tells you nothing about how much of that protein actually gets used by the body -- which in some cases can be very little.
Biological value (BV) measures how much of the protein that you eat gets incorporated into your body tissue. It does so by measuring how much of the nitrogen in the protein you eat is absorbed by the body and then how much is excreted. The assumption is that the difference is what got incorporated into your body protein. Its weakness is that BV varies greatly depending on how food is prepared and according to what other foods were eaten in the recent diet that can alter nitrogen measurements. Although the following three methods all provide better measures of protein utilization, BV is still commonly used by nutritionists out of force of habit.
Net protein utilization (NPU) is the ratio of amino acids converted to proteins to the ratio of amino acids supplied in the protein source. Experimentally, this value is calculated by determining the amount of dietary protein you are consuming and then measuring how much nitrogen is excreted. It is significantly affected by the limiting amino acids (as discussed earlier) in the particular food.
Protein Efficiency Ratio (PER) is based on the weight gain of a test subject divided by its intake of a particular food protein during the test period. Theoretically, it is a biological assay of the quality of a particular protein, measured as the gain in weight of an animal per gram of a particular protein eaten. At one time, this was the industry standard, but unfortunately PER is based upon the amino acid requirements of growing rats, which differ noticeably from that of humans.
Protein digestibility corrected amino acid score (PDCAAS) evaluates protein quality based on the amino acid requirements of humans. This is now the preferred standard. Nevertheless, it too has holes.
- PDCAAS takes no account of where proteins have been digested and cannot account for proteins that are absorbed by bacteria in the digestive tract.
- PDCAAS is calculated solely on the basis of single protein consumption and therefore once again does not calculate the changes in protein utilization resulting from the intake of complementary protein sources.
Improving Protein Utilization For Optimum Heatlh
Now Let's take what we've covered so far and see if we can extract some benefit from it that will help us improve our ability to improve the utilization of the protein we eat.
Consume More Than One Type Of Protein
As we've discussed, protein utilization is defined, to a large degree, by the limiting protein in the diet. Even complete proteins (those containing all of the essential amino acids) can still be out of balance so as to limit maximum utilization. Although dairy and egg tend to be well balanced and largely avoid this problem, they present other issues as we will see in subsequent parts of this series on protein. Meat, chicken, and fish, on the other hand, can benefit from the consumption of other proteins that help balance them out. And soy, most definitely.
Take Supplemental Digestive Enzymes With Your Dietary Protein
This can make a huge difference when it comes to facilitating your body's ability to break down complex proteins and eliminating the byproducts of incompletely digested proteins from previous meals. We will discuss this more in the next part of the series when we talk about protein allergies.
- An overview of enzymes
- Digestive enzymes
Watch What You Eat With Your Proteins
Some of the theories behind food combining may not be scientifically supported, but empirically the concept works.
And this is probably a good place to take a break and end this newsletter. When we continue our series on protein we will:
- Compare different protein sources
- Explore the nature of protein allergies
- Talk about how much protein you actually need
- Examine some "special conditions" related to the over-consumption of protein and the use of the wrong kinds of proteins
- And finish by looking at the ideal protein
Material originally published at www.jonbarron.org.
Copyright © 1999-2011. Baseline of Health® Foundation
Used by permission of the Baseline of Health® Foundation.
All rights reserved worldwide.
By: Jon Barron
Protein, Part 2 - Comparing Proteins
Many people think that the usability of protein is a question of animal versus vegetable. In fact, a number of people sent in comments off the last newsletter and stated as much -- that animal protein is better than vegetable protein. And yes, as a general rule, animal protein is "more complete" than many vegetable proteins, but that does not automatically make it better. For example, beef contains only about 20% usable protein. Spirulina and chlorella, on the other hand, average 75-80% -- and are just as complete and just as bioavailable. Combine the right yellow pea and rice protein and you can hit numbers approaching 85-90% usable protein -- again with high bioavailability. In the world of protein, nothing is necessarily what it first seems. In fact, the issue of animal versus vegetable is one of the least important determiners when it comes to protein usability.
Another factor to consider when we compare proteins is that there really is no such "thing" as dairy protein or whey protein or soy protein or any other "type" of protein, for that matter. Each source of protein is actually a conglomeration of several protein fractions that we lump together under their source name. Dairy protein, for example, actually describes a group of proteins that includes casein (which itself is a conglomeration of alpha caseins 1&2, beta casein, and kappa casein), alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin. Soy protein, likewise, is a mix of a number of protein fractions, although the names for the soy fractions are more utilitarian than for dairy, less prosaic if you will. Soy protein fractions include: 28 kD, 30-34 kD, 37 kD, 49 kD, and 50 kD. it's not necessary to know the names of all the different protein fractions in the different types of protein, but it is vital to know that they exist. Why? Because the different fractions have different degrees of digestibility and promote different degrees of allergic response. The prime culprit in soy, for example, is 30-kD allergen (Gly m Bd 30). Ultimately, the quality of a protein source (and its tendency to cause allergic response) is determined by how your body handles each and every fraction in that source. Which brings us to the issue at hand.
The efficiency, or degree to which dietary proteins can be used for building parts of the human body, is determined by five primary factors, most of which we described in the last issue of the newsletter Protein Part 1 of the series :
- The type and relative amounts of amino acids -- particularly any shortage of a needed essential amino acid.
- The size and structure of the protein molecule itself. (This relates to our discussion of protein fractions immediately above.)
- The amount of branched chain amino acids (BCCAs) present. BCCAs are defined by their unique structure and include leucine, isoleucine, and valine. These three amino acids are special in that they are metabolized in the muscle as opposed to the liver. The greater their presence in a protein, the higher the protein's bioavailability.
- Leucine is the most readily oxidized BCAA and therefore the most effective at causing insulin secretion from the pancreas. It should be noted that too much leucine can disrupt the tryptophan/niacin pathway and contribute to pellagra . It may also increase ammonia levels in the body.
- Isoleucine stabilizes and regulates blood sugar and energy levels.
- Valine assists in muscle metabolism, tissue repair and the maintenance of proper nitrogen balance in the body. However, too much valine can cause crawling sensations in your skin and hallucinations.
- How the protein comes packaged with other components such as pectin that may inhibit its digestion.
- The lack of enzymes necessary for the breakdown of that particular protein.
But beyond bioavailability, we also need to consider factors such as allergies and digestive problems such as gas, bloating, and constipation. In truth, it doesn't matter how "good" a protein is if you can't eat it.
Animal Versus Vegetable Protein
Obviously, dismissing the issue in a sentence is not going to cut it, so Let's spend a moment exploring the issue animal versus vegetable protein. Also, I'm not going to express an opinion on the morality or ethicality of eating meat -- although I definitely have one. My purpose in this newsletter is merely to evaluate the value of different protein sources, particularly as they relate to their use as a "supplemental" protein source.
As I've already said in I, protein bioavailability has much to do with the type and relative amounts of amino acids present in a particular protein molecule. Yes, the body has the ability to convert and make many of the amino acids it needs, but the nine essential amino acids cannot be manufactured by the body and must be supplied by the food we eat. Most animal proteins, by definition, contain all of the essential amino acids in sufficient amounts. The protein of cereals, most beans, and vegetables may contain all the essential amino acids, but the amounts in these plant foods is often less than ideal, particularly the branch chain amino acids. However, this is easy to compensate for, and it is possible to get plant proteins that are extremely concentrated. With that in mind, Let's take a look at the primary sources of protein and their pros and cons.
When most people in the developed world think protein, they think beef. We're talking steaks, hamburgers, hot dogs, roast beef. We're talking "hungry man food." If you have any doubt, just look at pictures of a training table for most athletes. But how good is meat as a primary source of protein?
On the plus side, it's complete. It contains all the essential amino acids. And it's not particularly allergenic. On the other hand, it's not particularly concentrated -- containing only about 20% usable protein by weight. And it's not particularly nutrient dense, inflicting a significant number of calories on your body along with the protein. It also tends to promote colon cancer -- particularly if grilled at high temperatures . And unless you're buying organic grass fed beef (you absolutely want organic ), it also comes complete with high levels of antibiotics, pesticides, hormones, an unhealthy ratio of Omega-6 to Omega-3 fatty acids, and the risk of E. coli contamination -- not to mention high levels of saturated fat.
You'll get about 23 grams of protein in a three ounce serving of beef, along with about 15 grams of fat. The biological value is about 70, and the net protein utilization is about 73.
Chicken and turkey are considered the "lighter," "less expensive" alternatives to beef. And in fact, lean turkey or chicken, without the skin, will provide about 27 grams of protein in a three ounce serving, along with about 2-3 grams of fat. Poultry has a biological value of about 80.
But, unless you're eating organic, it also contains large amounts of antibiotics, arsenic (oh yes, it's a government approved additive), and of course chicken leukosis cancer tumors.
Fish is a good high protein food. It contains reasonable amounts of quality protein, virtually no carbohydrates, and little saturated fat. Although the amount of fat and protein are about equal (5 grams in a 3 ounce serving), the fats tend to be highly beneficial Omega-3 fatty acids. Depending on the type of fish, its biological value ranges from 70-80, and it has a net protein utilization of 81, about the same as that found in poultry.
Unfortunately, if wild caught, it's likely to have high levels of mercury, and if farm-raised, high levels of antibiotics and dioxin.
I have to admit, the pork industry has had two of my favorite ads of all time. Back in the late 80's, to help turn around declining demand for pork, the National Pork Board launched their remarkable repositioning campaign, "Pork, The Other White Meat." It worked. The campaign effectively made people equate pork to chicken, as opposed to beef.
Then came the bird flu scare, and suddenly any association with chicken was unacceptable as millions of chickens were being slaughtered worldwide to prevent the spread of avian flu. At that point, the pork producers launched their, "Pork, it's Not Chicken" campaign.
You actually have to admire such shamelessness.
- The old dictum that pork is unhealthier than beef or chicken simply is no longer true -- unless you are still eating pork raised in a third world country that allows pigs to feed on garbage -- or corpses for any of you who saw the movie Snatch.
- Also, the old myth that pork is more indigestible than meat is likewise not true. That was just another way to warn people off pork when it was garbage fed. In fact, pork is slightly more digestible than beef.
- But it's also slightly higher in fat.
- It has all of the other problems associated with meat -- high in antibiotics, etc.
- And "free range pork" is remarkably rare. Virtually all of the pork available in the United States comes from animal factories that are inherently cruel, literally driving the animals mad in response to their "living" conditions.
The National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) estimates that 30 to 50 million Americans are lactose intolerant . These are people who cannot digest lactose, the sugar found in dairy products. According to the FDA , symptoms include gas, stomach cramps, diarrhea, etc. However, many others are also allergic to dairy products (lactose intolerance is not technically an allergy), specifically the proteins found in milk. In any case, these poorly digested bovine antigens (substances that provoke an immune reaction) like casein become "allergens" in allergic individuals. Dairy products are one of the leading cause of food allergies, often revealed by diarrhea, constipation and fatigue. Many cases of asthma and sinus infections are reported to be relieved and even eliminated by cutting out dairy. The exclusion of dairy, however, must be complete to see any benefit. An 8 oz glass of milk will provide 20-26 grams of protein and 5-10 grams of fat. It has biological value of 80-90 and a net protein utilization of about 81.
In previous natural health newsletters, I have made no secret of my antipathy when it comes to drinking milk, or using it as a primary source of protein, so I won't repeat it here.
When it comes to protein supplementation now, whey is king. It has pushed aside milk based protein supplements, egg proteins, and soy proteins to totally dominate the field. Why? Quite simply is has an extremely high biological value ranging from 90-100 for whey concentrate and from 100-150 for whey isolate. it's also high in the branch chain amino acids and is quickly absorbed by the human body.
Unfortunately, it's also highly allergenic. The problem isn't lactose or casein (a major allergen in milk) since they are both either removed or at significantly reduced levels in whey. However, the main protein fractions in whey (beta-lactoglobulin, alpha-lactalbumin , and bovine serum albumin ) are all highly allergenic. In addition, whey tends to have much more cholesterol in it than would normally be recommended.
A question worth considering is how many people are actually allergic to dairy and whey? Officially, that number is only about 1-3%. However, when you redefine that number to include anyone who generates extra mucous from eating dairy, suffers from constipation from eating dairy, or feels bloated after eating dairy, you're probably looking at numbers closer to 60-70%. And if you actually expand the number to include anyone who suffers from mild systemic inflammation after eating dairy -- and thus retention of water -- I believe that number approaches 100%. There are no official studies to support these numbers; they are just the numbers I have seen working with athletes, martial artists, and even bodybuilders over the last four years.
And finally, whey contributes to two conditions, aminoacidemia and intestinal toxemia, that we will talk more about in our next issue of the newsletter.
As a side note, the entire whey industry results from a desire to extract commercial value from what was once a waste product of the cheese industry. When you curdle milk to make cheese, it splits the milk into two components, curds and whey. The curd is the "solid" part that's used to make cheese. The liquid whey used to be considered a waste product, but then manufacturers began to heat the whey to evaporate the water and concentrate the protein in it. Now, there are more advanced filtration techniques available to concentrate the protein down and leave it in forms, such as whey isolate, that are more readily used by the body. But it still has many of the same problems.
At one time, before sophisticated whey processing emerged, eggs were considered the optimum protein supplement. In fact, the whole biological value scale is based on egg protein ranking a benchmark 100. However, eggs are arguably the most allergenic of all proteins . Oh, and for those of you who eat only egg whites, it should be noted that the allergenic proteins are concentrated in the egg whites.
And finally, because of their high sulfur content, eggs make for really smelly intestinal gas. Though this is not necessarily a major problem if you're a single bodybuilder with no plans to ever marry or meet anyone socially.
Egg Whites VS Whole Eggs
Okay, while we're on the subject, Let's talk about the myths associated with eggs.
First of all, contrary to popular belief, because whole eggs have a better amino acid profile than egg whites, the protein is more bioavailable in whole eggs than in egg whites. Whole eggs are also much more nutrient dense than egg whites since egg yolks contain all of the vitamins, minerals, antioxidants, and Omega-3 fatty acids (if you're eating free range chicken eggs). In fact, other than protein, egg whites are pretty much nutrient dead. And as for cholesterol concerns, recent studies do not support them.
But, all that said, the protein in eggs is still highly allergic and makes for very smelly gas.
Soy protein is not an effective alternative. It is high in allergens (some 28 different proteins present in soy have been found to bind to IgE antibodies). it's also worth noting that the more soy protein you eat, the more likely you are to develop allergies to it -- and the more severe those allergies are likely to become. Soy also blocks the absorption of important minerals such as calcium unless the phytates have been removed, and soy contains high levels of phytoestrogens, which although beneficial in moderate amounts, can be counter-productive in large amounts -- particularly for children.
In addition, although its biological value is not bad at 70 to 80, it's net protein utilization at 61 is quite low. In fact, unless it has been fermented, soy protein contains potent enzyme inhibitors that block the action of trypsin and other enzymes needed for protein digestion. This can create significant amounts of gas, in addition to promoting pathological conditions of the pancreas, including cancer.
As a side note, soy protein was once considered a waste product of the soy oil industry and used almost exclusively as cattle feed.
Spirulina is one of the great super foods. It is approximately 65 to 71 percent complete protein in its natural state. This is higher than virtually any other unprocessed food. (Note: whey protein, for example, has to be extracted and concentrated from dairy to reach higher levels.) And unlike most other forms of protein, the protein in spirulina is 85 to 95% digestible; again, one of the highest levels available. And finally, since spirulina has no cellulose in its cell walls, it is extremely easy for the body to break it down. In fact, its amino acids are delivered to the body for almost instant absorption.
So what's wrong with it?
First, it's not inexpensive. Blue green algae (a specialized version of spirulina) runs $40-80 a lb. Generic spirulina runs $15-40 a lb.
But $15 a lb would not be too much to pay for a high quality protein source, except for the taste -- somewhere between seaweed and grass. In small amounts, 1-4 grams a day in capsule form, it's easy enough to take. But if you're an athlete or bodybuilder or someone looking to recover from injury or illness and looking for 70-200 mg a day of protein, eating that much seaweed and grass could be tough for most people to manage.
And finally, about 30% of the worlds' population can't handle spirulina -- being either allergic to it, or suffering from toxins present in the spirulina that may have been absorbed from the water (such as Klamath Lake ) in which the spirulina is grown.
I actually prefer chlorella to spirulina. Not only is it a great source of protein, just slightly less concentrated than spirulina, but it offers one significant advantage over spirulina. Chlorella is one of nature's great detoxifiers, binding to heavy metals and pesticides and carrying them out of the body. I use chlorella in formulas for heavy metal detoxification as it binds very strongly to heavy metals to eliminate them from the body. There is a problem, though. Again, like spirulina, about 30 percent of people cannot tolerate chlorella, so if it makes you nauseous you should definitely avoid it. Also like spirulina, chlorella is not inexpensive ($30 to 50 a lb). And finally, like chlorella, it has that seaweed grass taste thing going, which makes it tough for most people to eat enough of it to use as a primary protein supplement source.
Hemp Seed Protein
Hemp seed protein has some unique features. First, 65% of the total protein content of hemp seed comes from the globular protein edestin, which is easily digested, absorbed, and utilized by the human body. As a side note, it closely resembles the globulin found in human blood plasma, which is vital to maintaining a healthy immune system. As such, edestin has the unique ability to stimulate the manufacture of antibodies against foreign invaders. It is also hypoallergenic.
As a complete food, hemp seed is great, one of the super foods, but as a protein supplement, less so. As straight ground hemp seed, it is only about 30% protein. Even in concentrated form it will only push to around 50% protein. Also, although the proteins in hemp (edestin and albumin) are great immune builders, they are less effective as muscle builders.
Buckwheat, Millet, Beans, etc.
Yes, a number of grains and beans are technically complete proteins and can serve as a foundational protein for vegetarian diets. However, they tend to be unbalanced in their amino acid ratios. This means that you have to eat them in proper combinations -- and you have to eat more of them than of animal proteins to obtain an equivalent value.
They are great for what they are (foundational foods), but they are not adequate for use as a "protein supplement" as required by athletes, people looking to lose weight, senior citizens, or people looking to recover from a prolonged illness. To build muscle mass, you need a more concentrated source of protein and a better mix of branch chain amino acids.
Rice And Yellow Pea Protein
I admit that a combination of rice and yellow pea protein sounds unappetizing. And, in fact, straight rice protein tends to be chalky in texture and unpleasantly blah in taste. But if done right, the combination of rice and pea protein actually provides one of the best tasting protein concentrates available. With that in mind,
Standard cooked rice has a protein content of only 5% to 7%. To make concentrated rice protein, whole brown rice is ground into flour, then mixed with water. Natural enzymes are then added sequentially to break down and separate out the carbohydrates and fibers from the protein portion of the slurry. Since the process is enzyme based, temperature must be kept low to preserve the enzyme activity levels. Low temperature and chemical free processing prevent the denaturing of amino acids, as is frequently seen in soy and dairy processing. The end product is 80-90% pure, hypoallergenic, easily digested protein. After four hours, the body digests over 86% of all ingested rice protein, compared with about 57% for soy. In the end, rice protein has a biological value of between 70-80, a net protein utilization of about 76, and a total absorption ration of some 98%.
Note: rice protein is high in the amino acids cysteine and methionine, but tends to be low in lysine, which negatively impacts its bioavailability. If you can raise its lysine levels, you can dramatically increase its bioavailability.
When it comes to perception, more people have a problem with the "idea" of pea protein than with rice protein. But in fact, pea protein has a very mild, pleasantly sweet taste. it's
one of the better tasting proteins.
Pea protein is the concentrated natural protein fraction of yellow peas. The process used for concentrating pea protein is water based, making the end product very "natural."
The Combination Of Rice And Pea Proteins
As mentioned above, rice protein is high in cysteine and methionine, but tends to be low in lysine. Yellow pea protein, on the other hand, tends to be low in the sulfur containing amino acids, cysteine and methionine -- but high in lysine. The bottom line is that when used in combination, rice protein and yellow pea protein offer a Protein Efficiency Ratio that begins to rival dairy and egg -- but without their potential to promote allergic reactions. In addition, the texture of pea protein helps smooth out the "chalkiness" of rice protein. Like rice protein, it is hypoallergenic and easily digested.
|Amino Acid Profile||Whey Protein||Rice/Pea Protein|
|Leucine (percent of total)||8||7|
|Isoleucine (percent of total)||6||4|
|Valine (percent of total)||5||4|
I have been using the rice/pea protein blend in various foods and supplements for over 4 years now. The results have been spectacular. In the next issue of the newsletter, I'll talk more about my work in developing a pure high protein supplement based on rice and pea protein that is producing some remarkable results among athletes, bodybuilders, senior citizens, and people looking to lose weight -- and it also happens to be blowing the competition away in comparison taste tests.
Let's conclude Part 2 of our series on protein with a discussion of how much protein your body actually requires. To begin with, you can throw the standard protein recommendations out the window. Most of the standards have holes in them so big you could drive a combine harvester through them.
For example, the Daily Reference Value (DRV) standard proposed by the FDA is based on a protein evaluation as a percentage of calories consumed -- with no consideration as to whether or not the calories being consumed are appropriate for the particular person consuming them. On average, the DRV for protein works out to about 50 grams per adult on a 2,000 calorie a day diet, regardless of age or sex.
The older RDA standard, on the other hand, is based on age and sex with a vague acknowledgement that special periods such as pregnancy and injury require higher levels of protein -- but no consideration for athletes or seniors, and no consideration of overall calories consumed.
|1 to 3||23||11 to 14||46||11 to 14||45|
|4 to 6||30||15 to 18||46||15 to 18||56|
|7 to 10||34||19 to 22||44||19 to 22||56|
On the other hand, if you go to most protein supplement sites, you will find much higher recommendations based on body weight ranging from 0.8 grams protein per kg of bodyweight to 1.2-1.8 g/kg. For a 70 kg adult (154 lbs) that works out to over 100 grams of protein a day -- and according to some recommendations, as much as 300 grams a day. But can a 150 lb adult who weighs 300 lbs because they are obese really need the same amount of protein as a 300 lb football linebacker -- even if they both theoretically "work out" every day?
The truth is that most people in the developed world eat more protein than they need. Food consumption surveys show an average protein intake of approximately 100 grams per day (regardless of body type, sex, or exercise levels), with about 70% of that from high fat animal products. Most people could do with significantly less protein per day (about 45-55 grams per day is adequate for most) -- but ideally from a "cleaner" source than they are now opting for.
Then again, people with special needs such as performance athletes, active adults, senior citizens, and people recovering from illness or injury may have requirements that run up to as much as 70-100 grams a day. Beyond that, we're talking about bodybuilders looking to put on as much muscle mass as is humanly possible. And when it comes to that, each bodybuilder knows their own requirements. But even there, I would recommend exploring hypoallergenic sources. (Eliminating allergens, eliminates water retention, which improves muscle definition.)
And that's it for now. In the last part of the series, we'll talk about:
- Protein Allergies
- Intestinal Toxemia
- And take a closer look at what I consider to be the ideal protein supplement
Material originally published at www.jonbarron.org.
Copyright © 1999-2011. Baseline of Health® Foundation
Used by permission of the Baseline of Health® Foundation.
All rights reserved worldwide.
By: Jon Barron
Protein Supplementation, Part 3 - Problems With Protein
Allergies, food intolerances, aminoacidemia, and intestinal toxemia are all problems that can accompany protein supplementation. They are also all factors to consider when choosing a protein supplement. The bottom line is that choosing the right protein supplement is not necessarily as simple as comparing product labels in a store.
Allergies And Intolerances
Protein digestion begins in the stomach. If the food you eat is not cooked or processed, enzymes present in the food itself will actually break down some 70% of the protein in the first hour in a process called autolytic digestion. After the first hour, pepsinogen and hydrochloric acid are introduced to the process (the hydrochloric acid converts the pepsinogen into pepsin). Pepsin further breaks down the protein into amino acids and their derivatives, a process that is completed (theoretically) by the enzymes trypsin and chymotrypsin produced in the pancreas and released into the small intestine. The amino acids and related molecules derived from the dietary protein are then absorbed through the walls of the gastrointestinal tract. The absorption rate of the individual amino acids is highly dependent on the protein source. For example, after whey protein is broken down, some 90% of it is absorbed quickly -- perhaps too quickly -- whereas soy protein is absorbed much more slowly and much less completely. A rice and pea protein combination, on the other hand splits the difference -- sharing soy's longer absorption time frame, but whey's high level of ultimate absorption.
This process, however, is not equal in all people. How the food is cooked, whether or not the protein is denatured by processing and heat, the presence or absence of enzymes (natural or supplemented), and the presence of other substances such as pectin can all affect the ultimate break down of the proteins and whether or not they trigger allergies or are responsible for intolerances. Which brings us to the question at hand.
Technically speaking, food allergies and food intolerances are two different things. A food allergy, or hypersensitivity, is defined as an abnormal response to a food triggered by the immune system. Common symptoms, according to medical authorities, usually appear within minutes to at most a couple of hours after eating the food in question and include:
- Tingling Sensation In The Mouth
- Swelling Of The Tongue And Throat
- Difficulty Breathing
- Abdominal Cramps
- Drop In Blood Pressure
- Loss Of Consciousness, And Death.
A food intolerance, on the other hand, does not involve the immune system (theoretically), occurs in the digestive tract, and is characterized by symptoms such as gas, bloating, constipation, diarrhea, headaches, and dark circles under the eyes.
In truth, food allergies and intolerances are two sides of the same coin (the inability to break down the food in question) manifesting in different parts of the body. If the protein in question is so large that it can't pass through the walls of the intestine and the symptoms they cause manifest in the intestinal tract without involving the immune system, they are called an intolerance. On the other hand, if the protein breaks down enough to pass through the walls of the intestine and enter the bloodstream, but allows for relatively larger proteins (larger than its constituent amino acids) to enter the bloodstream and be targeted as antigens by the immune system (or affect mast cells in the intestinal wall), you have a food allergy. Two parts of the immune response are involved;:
- The antibody, immunoglobulin E (IgE), that circulates in the blood.
- And mast cells, which can be found in all body tissues but especially in the nose, throat, lungs, skin, and gastrointestinal tract.
The most common food allergies are shrimp, lobster, crab, and other shellfish, nuts of all kinds (peanuts, walnuts, and tree nuts), wheat, corn, dairy, fish, and eggs.
The official line is that only about 1.5 percent of adults and up to 6 percent of children younger than 3 years in the United States -- about 4 million people -- have a "true" food allergy, according to researchers. But the reality is most likely quite different. Setting aside for a moment the 150 or so people who die every year from food allergies in the US, you can make a case that virtually 100% of people have a low level allergic response to foods such as wheat, corn, and dairy. By low level, I'm talking about almost immeasurable systemic inflammation in the body and chronic mucous production -- either seen in the stools, or experienced as constant throat clearing, sniffling, and high susceptibility to allergy triggers such as dust and pollen.
This is based on personal experience and my observation of thousands of people over the 40+ years I've been working in alternative health. From personal experience, I had severe allergic responses to pollen and dust into my 30's. Only after several complete body detoxes and a change in diet (cutting way back on wheat, corn, and dairy) did those allergies to dust and pollen disappear. Now, no allergies, unless my diet is very bad several days in a row -- at which point my wedding ring no longer slides easily off my finger (low-level, systemic inflammation) and my nose starts to plug. One day of juice fasting, and the swelling goes away. Over the years, I have seen thousands of people parallel this scenario. The numbers are far higher than officially acknowledged. It just depends on what symptoms you're looking for. On another note, the official line is that food allergies are genetically based. Maybe so, but the use of detoxing and changes in diet can dramatically alter any manifestation of those genetic tendencies.
Ultimately, allergies are not restricted to proteins. Almost anything can trigger an allergic response in a susceptible individual -- for example sunlight (solar urticaria) and water (aquagenic urticaria) can trigger responses in a small number of people. But dig deep enough, and a protein may still play a prominent role -- as can be seen in solar urticaria.
For the purposes of this newsletter, though, our focus is on dietary proteins and protein allergies. With that in mind, the primary culprits are:
- Dairy And Whey
- Shell Fish
- And Wheat Gluten Meat Substitutes For Vegetarians
But concerns about protein consumption do not end with food allergies and intolerances. There are a couple of other conditions that need to be mentioned:
- Intestinal Toxemia
Aminoacidemia may sound like a disease, but it's not. it's merely a condition in which excessive amounts of amino acids are present in the blood. What it means depends on what caused it. If there is nothing in the diet, for example, to account for it, it could be indicative of missing or defective enzymes in the liver, which are essential for the breakdown of nitrogen containing amino acids in the body. If your body can't sufficiently break down amino acids, it can lead to generalized hyper aminoacidemia, and ultimately to neurotoxicity and early death.
But if that's your problem, your doctors have most likely already dealt with it, or you're not reading this because you're already dead. So we're not talking about disease here. We're talking about intentionally induced aminoacidemia through diet. For years bodybuilders have claimed this is a helpful condition for building muscle, and for several years now, this has been one of the main selling features of whey protein in the bodybuilding community. The rational is that muscle growth is about staying in a positive nitrogen state. Exercise damages muscle, stresses it, and throws your body into a negative nitrogen catabolic (breakdown) state. And the best way to take yourself out of a catabolic state and into a positive nitrogen anabolic (building) state is to consume the fastest absorbing protein you can get your hands on -- whey. And there is no question that whey protein induces a short term dramatic increase in blood levels of amino acids -- i.e. aminoacidemia. Unfortunately, new studies now indicate that this rational, taken as a whole, may not necessarily be true.
Specifically, studies have confirmed the "paradox" of the highly soluble proteins found in whey and whey isolate, which, despite their high Protein Digestibility Corrected Amino Acid Score, ensure a rate of amino acid delivery that is too rapid to sustain the body's anabolic requirement during the minutes and hours after consuming it -- thus being counterproductive for the development of muscle. Or in simple terms, aminoacidemia may not provide the benefit many bodybuilders think it does.
But even worse, aminoacidemia may actually have long term health consequences. One example is diabetes. Interestingly enough, short term aminoacidemia can actually lower blood sugar levels since it stimulates higher beta cell secretion and a concomitant increase in insulin levels (by as much as 40%). This, of course, significantly lowers blood sugar levels. However, over time, this constant stimulation may overstress and degrade the ability of beta cells to produce sufficient insulin when called for and may ultimately, over time, contribute to pre-diabetic and diabetic conditions in the body.
In addition, excess amino acids are converted into carbon dioxide, water, and ammonia. Ammonia is toxic to the body and is a primary cause of premature fatigue. Normally, the body handles excess ammonia by converting it to urea then filtering it through the kidneys. But if the ammonia level is too high, it overburdens the kidneys. This is why doctors will insist on lower levels of protein intake in cases of kidney disease. And finally, although you can find studies all over the map on the question of high amino acid levels in the blood (i.e., high protein consumption) and bone loss, by far, the most convincing studies indicate that there is a problem.
Whey And Intestinal Toxemia
First, let me state that intestinal toxemia is not a medical condition. It is more of a catchall phrase used in the alternative health community to describe a set of conditions that can arise in the intestinal tract as the result of improper dietary choices. It has three primary manifestations:
- Putrefaction, which is caused by bacterial action on undigested proteins. Guanidine, histamine, mercaptans, indol, phenyl, skato, and other organic toxins may be formed as a result.
- Rancidity refers specifically to the spoilage of fats. This can actually occur in the digestive tract itself -- not just from the consumption of rancid fats in the diet. The primary concern is that rancid fats promote the production of peroxide free radicals in the body.
- Fermentation is caused by the action of bacteria and yeasts on carbohydrates. Excessive gas, increased blood alcohol levels (that's why excess sugar can give you a hangover), and Candida hyper-growth are just three problems associated with intestinal fermentation.
Intestinal toxemia occurs when large particles of undigested food enter the small intestine and colon. Since these parts of the digestive tract were not designed to handle excessive amounts of undigested food, the partially digested food mass becomes a fertile breeding ground for bacteria and yeast fermentation. Each nutrient degrades in its own unique way. Proteins putrefy, carbohydrates ferment, and fats become rancid due to the workings of intestinal bacteria. These bacteria then produce harmful by-products that damage the intestines, reduce nutrient assimilation, create excess gas and bloating, and lead to persistent diarrhea. On top of that, mild to intense stomach pains (the result of muscle cramping and excessive gas) accompany this process. Prolonged intestinal toxemia may be a major contributing factor in the onset of Irritable Bowel Syndrome and Crohn's Disease.
For a number of reasons, whey protein can be a major factor in promoting intestinal toxemia. Whey contains no fiber, which is necessary to keep things moving consistently through the intestinal tract. Because it is highly processed, whey protein contains no live enzymes to break down the large whey proteins. The human body actually has a hard time breaking down the three primary proteins in whey. Taken together, these problems provide an optimum environment for non-beneficial intestinal bacteria to thrive in. In addition, whey is very acid forming, which raises the pH of the normally alkaline environment of the intestinal tract, thus favoring the growth of unfriendly bacteria over beneficial bacteria.
So what's the best protein supplement?
Throughout this series on protein, we've explored a number of aspects of protein, including a detailed exploration of the pros and cons of each protein source. Let's now conclude the series by talking briefly about which protein is best for the majority of people looking to supplement their daily intake. Or to put it another way, for those of you who desire extra protein (athletes, bodybuilders, active adults, people looking to lose weight, seniors, people looking to recover from illness or injury, or people looking to rebuild lost muscle mass), what supplemental protein should you use?
The Rice/Pea Protein Combination
As I've mentioned several times throughout this exploration of protein, I've been working with rice/pea protein combinations for years. It was my protein of choice in my Private Reserve Superfood® Formula. Despite all its benefits, though, rice/pea protein has a problem -- taste and texture. Anyone who has used rice protein supplements can tell you that they pretty much taste awful and have a chalky texture that sticks in your throat. Pea protein has a milder taste, but doesn't blend very well with liquids. that's why you don't see them used very much in protein supplements (except those designed for dedicated vegans), and that's why it's taken almost 4 years of experimentation to be able to make those ingredients work in a standalone protein formula -- as opposed to being part of a super food blend as it is in Private Reserve .
In the end, though, after countless iterations and what seemed like almost endless trial and error, I got the combination to work, even better than I ever thought possible. In taste tests, a number of "protein aficionados" have said it is the single best tasting protein supplement they have ever used. And they can't believe we got the taste so pleasantly sweet without using any sugar, stevia, or artificial sweeteners. it's virtually non glycemic. And it adds a nice texture to any smoothie or drink that it's used in. But best of all, it avoids all of the problems associated with soy, dairy, whey, and eggs. Specifically, it's:
- No Burping
- No Bloating
- No Indigestion
- No Diarrhea
- No Constipation
- No Gas
- No Allergies
- Does Not Contribute To Aminoacidemia
- Does Not Contribute To Intestinal Toxemia
- Easy/Fast Digestion
- High Protein Content (75% by weight)
- 90% Absorption
- No Antibiotics
- No GMO
- No Estrogens
- No Cholesterol
I developed it for a company called Perfected Nutrients®, and they are planning to sell it under the name Nutribody Protein. They are currently wrapping up comprehensive product testing in all demographics before releasing it. In other words, it's not for sale yet -- but close.
For more information, you can go to their website at www.nutribodyprotein.com. Be sure and check out the ingredients, the research, and the testimonials -- many from top athletes. Their plan is to have the Nutribody Protein available for sale in the next few days. You can leave your name and email address on their website if you want to be notified exactly when and where it's available near you -- otherwise, you can just keep checking back on their website every couple of days to see when they announce its release.
Protein Information: Natural News 11/2/2009 - High Protein Diets May Lead To Brain Shrinkage
Protein Information: Natural News 8/17/2012 - Everything You Need To Know About Protein
Protein Information: Dr. Mercola 4/30/2000 - Pork Causes Illness
Protein Information: Dr. Mercola 7/23/2000 - Corn Proteins Found In Infant Formula
Protein Information: Dr. Mercola 1/14/2001 - High Protein Diet Found Beneficial
Protein Information: Dr. Mercola 12/11/2008 - High Protein Meals Can Help The Overweight Burn Fat
Protein Information: Dr. Mercola 5/11/2011 - The Protein Powder You Should Never, Ever Buy
Protein Information: Dr. Mercola 8/17/2011 - Muscle Building Protein Doubles As A Powerful Antioxidant
Protein Information: Dr. Ben Kim 6/1/2010 - Fuel Your Best Health With Healthy Protein