Free "Whey Protein Exposed" article

[robertthoburn]

Whey Protein EXPOSED
Did you know that there is compelling scientific evidence that whey protein is more 'anabolic' for your pet dog, rat, or chicken than you?

I guarantee my article will change the way you look at whey protein supplements forever.

If you'd like a copy, send me an e-mail. Give me the e-mail of addresses of 3 of your friends (so I can send it to them with your permission), and I'll give you the article for free.

No product promotions, just some scientific facts that I share in an attempt to make this industry more profitable for all parties involved.

Protein supplements can definitely offer convenience, but many of the claims attesting to muscle-building powers rest on shady misinterpretations of science.

Thanks,
Robert Thoburn

robertthoburn@hotmail.com

[windwords7]

LMAO, what a joke! You post the article and let your peers review it moron. That's how it works in the non-scammer world.

[Biggin]

*gasp* scammer?

[windwords7]

Well at the very least a Spammer. "Gimme three of your friends addresses"....ya ya ya.

[robertthoburn]

Where would you like me to post the article for the best viewing?

Thanks, everybody.

Robert Thoburn

[windwords7]

Post it right here.

[psikooz]

here bro..
just post it here

[Veritas]

....post....it....here......

[jonathan reeves]

bump

[eddie905]

Originally posted by robertthoburn
Give me the e-mail of addresses of 3 of your friends

robertthoburn@hotmail.com

I stopped reading after I read this, I say we sign him up on some gay porn mailing lists.

[Dannyboy5000]

taken care of =D

[robertthoburn]

WHEY PROTEIN ‘EXPOSED’
By Robert Thoburn

If you think that whey protein is superior to for bodybuilding purposes, you may be shocked when you read this article.

Accounting 101: Protein Balance
First, let’s begin by talking about accounting.

Protein, whether we’re talking about the protein that makes up your own tissues, or that supplied by food, consists of amino acids linked together in chains. Amino acids are the principle means by which we get nitrogen –an essential element in your survival.

Building bigger muscles is about balance –protein balance. If your body makes more muscle protein than it breaks down (i.e., a positive protein balance) your muscles will increase in size and strength with time. Conversely, if you make less muscle protein than you break down (i.e., a negative protein balance), your muscles will tend to get weaker and smaller.

Scientists refer to ‘building up’ (synthetic) processes as ‘anabolism’ or ‘anabolic’; ‘catabolism’, or ‘catabolic’ processes, in contrast, involve breaking down tissue structures. Thus, a positive protein balance indicates an anabolic state.

A Positive Protein Balance is Essential to Building Bigger Muscles
Since protein contains nitrogen, we can estimate your protein balance by measuring your nitrogen balance. Technically speaking, however, the two should not be considered equal. In any case, a positive nitrogen balance is generally taken as a sign of an anabolic state with an overall gain (retention) of nitrogen for the day, whereas a negative nitrogen balance indicates a catabolic state.

Another, arguably more accurate, way to estimate your protein balance is by measuring your body’s balance of a particular amino acid, such as leucine. A positive leucine balance indicates protein anabolism. Or, at least, a positive leucine balance reflects a state (i.e., increased availability of leucine inside your muscle cells) that supports protein anabolism. Conversely, a negative leucine balance suggests protein catabolism (‘breaking down’). Simply stated, a positive leucine balance is ‘good’; a negative leucine balance, ‘bad’, for the purpose of building bigger muscles.

Maintaining Muscle Protein Balance
You don’t eat all the time; there are gaps in your protein intake, such as in between meals and while you sleep.

So how does your body preserve its protein balance? How does it keep your ‘Protein Economy’ (the total amount of protein in your body) from shrinking --and your muscles alongside-- in the face of fluctuating intakes of dietary protein?

Your body maintains its protein balance largely by adjusting tissue protein breakdown according to how much protein you feed it (for review see Garlick et al., 1999).

In between meals (e.g., overnight), you lose tissue (e.g., muscle) protein, but after a protein-containing meal, you recoup what you lost through a decrease in protein breakdown. The production, or synthesis, of tissue protein often stays about the same after a protein-containing meal (Melville et al., 1989; Price et al., 1994; Garlick et al., 1999), yet because protein breakdown is reduced, the result is a net increase (gain) in protein such that balance is achieved. You don’t get bigger, but you don’t shrink, either.

In order to actually make your muscles bigger and stronger, you’ve got to work on both sides of the protein balance equation. However, the stimulation of muscle protein synthesis is by far the most important half of the muscle-building equation. This cannot be emphasized enough. Indeed, the stimulation of muscle protein synthesis is the means by which resistance exercise makes muscles grow (Barr and Esser, 1999); it’s also how some of the most powerful muscle-building hormones (e.g., testosterone, growth hormone, insulin-like growth factor-1) work their magic.

Whey vs. Casein
Now we’re prepared to discuss protein supplements. Whey and casein are the two major proteins in milk. Whey is frequently touted as the highest quality protein available for the bodybuilder or similarly-focused individual. Yet these claims appear to reflect a vast misinterpretation of the available scientific literature on the matter.

Absorption: Faster is Not Better!
When you eat a serving of whey protein, its digestion in your gut results in a very rapid, but short-lived, surge of amino acids into your bloodstream (Boirie et al., 1997). Casein, by comparison, yields a slower, more sustained release of amino acids (Boirie et al., 1997). Importantly, casein’s slower absorption profile seems to better promote a positive protein balance (Boirie et al., 1997) –an essential requirement for building bigger muscles.

Recall from above that one way of estimating your protein balance is by measuring your body’s balance of a particular amino acid, such as leucine. A positive leucine balance indicates a state (i.e., increased availability of leucine inside your muscle cells) that supports protein anabolism. Conversely, a negative leucine balance indicates conditions favoring protein catabolism.

Ironically, whey protein marketers have been known to cite the Boirie study (Boirie et al., 1997) as evidence with which to support whey’s ‘superiority’ as a muscle-building protein. Contrary to what their ads and articles (‘advertorials’) imply, however, Boirie et al. found that casein –not whey— produced the most positive leucine balance when fed to healthy young humans. In fact, whey actually produced a negative leucine balance.

The negative leucine balance associated with eating whey protein resulted from a greater loss of leucine, through its irreversible ‘burning’, or oxidation. Furthermore, when the subjects in the Boirie et al. study ate whey protein, more urea was formed than when they ate casein. Urea is a waste product of amino acid breakdown. Nitrogen from amino acid breakdown is irreversibly transferred to urea. Since urea cannot be reused, it represents a loss of nitrogen.

To sum it up, at least under the conditions of this study, casein demonstrated superior potential for promoting a positive protein balance as compared to whey –not the other way around. But even so, will this difference translate into faster gains in muscle size for you? Maybe. Maybe not. The answer must be determined by long-term, controlled clinical trials.

Whey’s Frequently Touted ‘Virtue’ Is Actually Its Downfall
Again, whey is often said to be superior to casein because of its ability to deliver amino acids into your bloodstream rapidly. Yet this is not a virtue; rather, it’s a weakness.

When it comes to amino acid absorption, haste makes waste. The rate at which amino acids are broken down, or catabolized, is directly related to the level they achieve in the bloodstream (Reeds et al., 1992). The faster the amino acids provided by the protein you eat exit your gut and enter your bloodstream, and the higher the blood levels they attain, the more they get wasted.

The higher your blood levels of the amino acid leucine, for instance, the greater its rate of catabolism. Eating whey protein drives blood leucine levels very high (Boirie et al., 1997). Not surprisingly, this results in a corresponding loss of leucine through catabolism (Boirie et al., 1997). And as indicated above, whey generates more urea –the waste product of amino acid breakdown— than casein.

[robertthoburn]

Barnyards, Hair and Feathers
There’s another longstanding issue we need to clear up. To do so, let’s go visit the animals in the barnyard. A barnyard filled with cows, sheep, dogs, rats, cats, chickens.

What do all these creatures have in common? And what the heck has this got to do with bodybuilding and whey protein supplements?

Plenty, in fact. To answer the first question, unlike you and me, all of above barnyard creatures are covered in either hair or feathers. Hair and feathers are made of the protein known as keratin, which is rich in the sulfur-containing amino acid, cysteine (found in keratin in its oxidized form, cystine).

Cysteine can be produced in animals from another sulfur-containing amino acid, methionine. Since whey has more sulfur-containing amino acids than casein, hair- or feather-covered animals require less whey than casein to achieve protein balance. But this advantage will clearly does not apply to humans, a relatively hairless and featherless species, as the Boirie et al. study would seem to agree.

Nevertheless, studies performed over a half-century ago on hair- or feather-covered animals which demonstrated the ‘superiority’ of whey over casein, have been used as marketing ‘support’ by companies selling whey protein supplements.

Back in 1947, Tomarelli and Bernhart demonstrated that feeding whey protein (hydrolyzed a-lactalbumin, more specifically) to rats produced greater protein retention than did casein (e.g., Tomarelli and Bernhart, 1947). The rats required about 70% more casein nitrogen than whey nitrogen per day to maintain nitrogen balance. These results are consistent with a number of similar studies performed around this time. The trouble is that these studies, too, were performed on animals covered either in hair or feathers –rats, dogs, and chickens, for instance. Thus, these data are applicable to barnyard animals, but not to humans.

Methionine is an essential sulfur-containing amino acid. As I noted earlier, it can be used by your body to synthesize cysteine (as in the production of keratin). Rats, which were commonly used in early studies to determine the frequently-quoted “Biological Value” (BV) of various dietary proteins, have a methionine requirement that is around 50% greater than you or I (Sarwar et al., 1989). This contributes to the lower BV numbers reported for dietary proteins containing relatively less methionine when such proteins are fed to rats, as compared to humans (Bricker and Mitchell, 1947).

Johnson et al. (1946) relate: “In the case of the human experiments, then, it would be concluded that the methionine requirement is lower, and is not a limiting factor in the attainment of nitrogen excretion in these experiments, or that the requirement is met by the body protein breakdown plus any dietary protein….Since the addition of further methionine did not reduce the nitrogen excretion on the low protein diet, it can be concluded that no more methionine is required under these circumstances than that represented by the entire sulfur excretion, or 1.4 gm methionine per day for our average subject….the present experiments suggest that the human body is not limited in its ability to conserve nitrogen by the need to meet a methionine requirement.”

Cox et al. (1946) clarify even further: “comparison of the nitrogen retention of a casein hydrolysate with and without added methionine in rats, dogs and man has clearly shown a striking species difference. The addition of methionine increased the rate of growth in rats and the magnitude of nitrogen retention in dogs. In man, however, it was without effect on nitrogen retention…An explanation for this difference does not seem difficult, based on the fact that the rat and dog are covered with hair, and that man is not. Since hair contains large amounts of cystine, it is reasonable to suppose that the requirement for this amino acid (or methionine) is considerably greater than that of man…The generally recognized nutritive difference between casein [lower in cystine] and lactalbumin [higher in cystine] is valid for the rat and for the dog, but not for man.”

CONCLUSION
As the above evidence hopefully makes clear, the claim that whey is superior to casein for building muscle is simply not valid.

The study performed by Boirie et al. (1997) found evidence to suggest that casein is superior to whey for promoting a positive protein balance. But that doesn’t necessarily mean it will build muscle any better than whey, or a chicken breast meat, for that matter.

Protein supplement ads and articles frequently cite Biological Value (BV) numbers (e.g., 104 and sometimes even higher) for whey as evidence for its superiority; however, these BV values were derived from studies on hair- and feather-covered animals that require more of the sulfur-containing amino acids that whey is rich in. These results do NOT apply to humans.


REFERENCES
Boirie Y, Dangin M, Gachon P, Vasson M-P, Maoubois J-L, Beaufrere B (1997). Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci USA, 94: 14930-14935.
Bricker ML, Mitchell HH (1947). The protein requirements of the adult rat in terms of the protein contained in egg, milk and soy flour. J Nutr, 33: 491-504.
Cox WM JR, Mueller AJ, Elman R, Albanese AA, Kemmerer KS, Barton RW, Holt LE Jr (1946). Nitrogen retention studies on rats, dogs and man: The effect of adding methionine to an enzymic hydrolysate. J Nutr, 32: 437-457.
Demling RH, DeSanti L (2000). Effect of a hypocaloric diet, increased protein intake and resistance training on lean mass gains and fat mass loss in overweight police officers. Ann Nutr Metab, 44: 21-29.
Fereday A, Gibson NR, Cox M, Pacy PJ, Millward DJ (1998). Variation in the apparent sensitivity of the insulin mediated inhibition of proteolysis to amino acid supply determines the efficiency of protein utilization. Clin Sci, 95: 725.
Garlick PJ, McNurlan MA, Patlak CS (1999). Adaptation of protein metabolism in relation to limits to high dietary protein intake. Eur J Clin Nutr, 53: S34.
Johnson RM, Deuel HJ, Morehouse MG, Mehl JW (1946). The effect of methionine upon the urinary nitrogen in men at normal and low levels of protein intake. J Nutr, 32: 371-387.
Melville S, McNurlan MA, McHardy KC, Broom J, Milne E, Calder AG, Garlick PJ (1989). The role of degradation in the acute control of protein balance in adult man: Failure of feeding to stimulate protein synthesis as assessed by L-[1-13C]leucine infusion. Metabolism, 38: 248-255.
Price GM, Halliday D, Pacy PJ, Quevedo RM, Millward DJ (1994). Nitrogen homeostasis in man: 1. Influence of protein intake on the amplitude of diurnal cycling of body nitrogen. Clin Sci, 86: 91-102.
Reeds PJ, Fiorotto ML, Davis TA (1992). Nutrition partitioning. An overview. In: Bray GA, Ryan DH, eds. The Science of Food Regulation. Volume 2. Baton Rouge: Louisiana State University. p. 103-120.
Sarwar G, Peace RW, Botting HG, Brule D (1989). Relationship between amino acid scores and protein quality indices based on rat growth. Plant Foods Hum Nutr, 39: 33-44.
Shigemitsu K, Tsjui****a Y, Miyake H, Hidayat S, Tanaka N, Hara K, Yonezawa K (1999). Structural requirement of leucine for activation of p70 S6 kinase. FEBS Lett, 447: 303.
Tomarelli RM, Bernhart FW (1947). A bioassay for protein and protein digests. J Nutr, 33: 263-272.

[brylac]

i always thought casein made you fat.

[pogue]

So what would be your suggestion? a 50/50 whey casein blend? or use casein completely instead of whey?

How does the amino acid profile of casein stand up against whey?

[DRACOMACHINE]

Your article backs up alot of what many of us tell newbies around here about protein. Whey has its place (Pre- and Post workouts). Yet a good protein blend is best for the rest of the day. (In addition to whole food choices as well) The blend of Whey, casein, egg, l-glutamine, will provide a good source of protein for your body.

This would be a good article for newbies to read. However there are many on this board that will see this article as something they already new and "Not ground Breaking" like you were pushing it. But it is a good article for those people starting out in the supplement world.

[ironjayc]

Ok, first of all, thanks for posting the article here for our convenience

And to be honest with you, the protein sources you mentioned(Whey, Casein) have to be used to your advantage in different, specific situations in order to acheive optimal muscle-building results. For instance, you generalizingly compare Casein to Whey in terms of "Building Muscle". Well, despite Whey's obvious higher biological value, Casein is slower digesting, and therefore more effective for use as a "Main Protein source". Whey should be used, in my opinion, at the "Muscle Building Window" times, such as immediately upon waking, or immediately after a workout where you need quick absorption for the very best in gains. Casein(or other slow digesting proteins, such as Chicken, tuna, or beef) should be ingested every 2-3 hours on top of the 2 critical windows that i've previously mentioned where amino acid uptake by the body is dramatically increased.

So by taking advantage of the body's specific time and demand, you can only get optimal results using BOTH Whey and Casein. Basically what it can also mean, is that too much of one thing isn't good, and moderation should be combined with intelligence in order to create the very best atmosphere for muscle building in your body.

References: IronJayC()

[robertthoburn]

Thanks for your comments, people.

The most important issue is not that of amino acid absorption rates. Rather, it is the "barnyard animals" studies I cite.

A key premise of whey protein supplementation is that whey has the highest biological value (BV), and is thefore best for building muscle mass in humans.

As I indicate in the article, the BV of whey was demonstrated on animals with distinctly different amino acid requirements than us. In particular, these were hair or feather-covered animals with higher requirements for cysteine, a key component of keratin in hair and feathers.

Whey supports cysteine balance better than does casein, and that's why those BV studies found it to have a higher utility.

In humans, none of this matters.

If you think protein powders are convenient, then by all means.

I use no protein supplements whatsoever. Myself, I have found the 'secret' to be to train in an appropriate manner for building muscle (as opposed to strength). I'm exceedingly strict with diet, but the key in this regard is not eating too much yet getting enough carbohydrate to keep my muscles full.

You guys are a tough crew....very well educated on these matters!

Best,
Robert Thoburn

[DRACOMACHINE]

The most important issue is not that of amino acid absorption rates. Rather, it is the "barnyard animals" studies I cite. "robertthoburn"



Oh! So the animal study was your primary area of concern. It was cool to read about the effects on feathers and hair covered animals.

Hey, maybe you can get ironjayc to write an article with you. he had a lot of info that you could use.

[ironjayc]

Originally posted by DRACOMACHINE
Hey, maybe you can get ironjayc to write an article with you. he had a lot of info that you could use.

lol, hey thanks for the shout-out man!

And RobertThoburn, i'm not sure how many barnyard animals we have browsing the Bodybuilding boards, but i'm sure they'd be MORE than excited when they come across your article. And hopefully future articles too, because then they could hear the latest groundbreaking news on how to keep their hair/feathers as shiny/healthy as possible(naturally, that is)!

[DRACOMACHINE]

Research is now showing that really hairy people might benefit more from Whey protein, then those people who shave. Since body hair needs the extra sulfer proteins it could be usefull to those striving for the unzipped shirt, exposed hairy chest look of the seventies. The look that would excite Janet and Chrissy down at the Regal Beagle!

[CrAvEnCLiCK666]

what the fuk? so only use whey upon waking and post workout at all other times try to use animal protein?

[AznBB]

Originally posted by CrAvEnCLiCK666
what the fuk? so only use whey upon waking and post workout at all other times try to use animal protein?

Yes, whey is really only useful at times when your body needs a quick stream of amino acids such as upon waking and postworkout. At all other times you want some slow digesting proteins like Casein or meat proteins...

[DRACOMACHINE]

Exactly! I guess good things are coming from this thread, I did not realize so many people did not understand how and when to take Whey protein.

Advertisements do not help. You always see companies pushing meal replacements that are 100% superior whey protein. Muscle-tech, Twin lab- RX ,and Labrada. They only pushed the whey protein to try and take customers away from EAS and Met-rx.

[institutional]

who are you? and what is your angle or motives? btw interesting article, but not groundbreaking news.

[Number 5]

robertthoburn,

interesting article, and there's more evidence to back casein over whey. i will post one, originally posted by bobo, at anabolicminds, at the end of this post. also, what i find interesting are the claims by many pros not to use these products (protein powders), just real food & real test.

i prefer whey only after my workout b/c it's claimed that your muscles need proteins fast during the post-workout window, and whey is absorbed fastest. i take it you disagree with this evaluation, please elaborate.

the other advantage of whey is that it mixed better and tastes better than any other protein i've tried, but that's beside the point.

-5

bobo's post:

Effect of a hypocaloric diet, increased protein intake and resistance training on lean mass gains and fat mass loss in overweight police officers.

Demling RH, DeSanti L.

Brigham and Women's Hospital, Boston, MA 02115, USA. rhdemling@partners.org

We compare the effects of a moderate hypocaloric, high-protein diet and resistance training, using two different protein supplements, versus hypocaloric diet alone on body compositional changes in overweight police officers. A randomized, prospective 12-week study was performed comparing the changes in body composition produced by three different treatment modalities in three study groups. One group (n = 10) was placed on a nonlipogenic, hypocaloric diet alone (80% of predicted needs). A second group (n = 14) was placed on the hypocaloric diet plus resistance exercise plus a high-protein intake (1.5 g/kg/day) using a casein protein hydrolysate. In the third group (n = 14) treatment was identical to the second, except for the use of a whey protein hydrolysate. We found that weight loss was approximately 2.5 kg in all three groups. Mean percent body fat with diet alone decreased from a baseline of 27 +/- 1.8 to 25 +/- 1.3% at 12 weeks. With diet, exercise and casein the decrease was from 26 +/- 1.7 to 18 +/- 1.1% and with diet, exercise and whey protein the decrease was from 27 +/- 1.6 to 23 +/- 1.3%. The mean fat loss was 2. 5 +/- 0.6, 7.0 +/- 2.1 and 4.2 +/- 0.9 kg in the three groups, respectively. Lean mass gains in the three groups did not change for diet alone, versus gains of 4 +/- 1.4 and 2 +/- 0.7 kg in the casein and whey groups, respectively. Mean increase in strength for chest, shoulder and legs was 59 +/- 9% for casein and 29 +/- 9% for whey, a significant group difference. This significant difference in body composition and strength is likely due to improved nitrogen retention and overall anticatabolic effects caused by the peptide components of the casein hydrolysate. Copyright 2000 S. Karger AG, Basel

[robertthoburn]

Sorry, guys. I simply won't be able to answer all of your questions directly.

Not that I don't read them. You all impress me as a very discerning and insightful bunch of people, so your questions and comments I find to be valuable.

As far as my motives, I operate a scientific and marketing consultancy. My specialty lies in translating basic research into new product concepts (product positioning concepts, formulae) and marketing communciations (ads) with which to sell them.

I've been bodybuilding since I was 16, and I love it. That's why I chose to make it my full-time 'gig', as it were.

I enjoy sharing my knowledge (and letting you guys criticize it), because it allows me to build upon it. At the same time, it helps me build equity in my name. After all, as a consultant, that's what I survive on.

I offer, I feel, a unique perspective, having been on the scientific (R&D) and marketing (brand management) side of the business. I've written some of the ads you see out there, and helped develop some of the products.

I'm busy with my work, so again, I won't be able to answer all your questions. But, every now and then I'd like to share some of my ideas with you. And when I have time to answer your questions, I most certainly will.

Thanks for providing me with the opportunity to build a career around the game of bodybuilding!

Best,
Robert Thoburn

[jonathan reeves]

roberthoburn: So as far as protein after workout and when you wake up what do you use. Obviously in these cases Whey is still the ideal protein

[robertthoburn]

Thanks, Jonathan, for reading my article.

Why do you feel whey is the 'best' protein.

I don't use any protein supplements. I find I get the best results by working out in a way that stimulates muscle growth efficiently and eating a low-fat, high-carbohydrate diet.

In fact, I don't eat until I've done my workout, usually in the late morning.

In experimenting with protein supplements heavily over the years, I actually swore that whey made me fat. Granted, calories in, calories out. Still, some calories have more of a tendency to slam the brakes on your fat-burning metabolism, thereby increasing the risk of fat gain. I think some whey protein supplements are in this category.

Here's an interesting, albeit teleological observation: Beef is skeletal muscle. This is de facto proof that its amino acids are well suited for building muscle tissue. Compare that with a heavily processed whey protein powder.

Now, humans got to this point in the Darwinian race because of their ability to survive on just about any kind of diet reasonably well (good enough, at least). Thus, we can certainly build muscle with protein from whey, as we can from the protein found in plants.

Nevertheless, I point out my 'beef as de facto proof' example to spur some possibly valuable exercises in thought.

You can get a feel for what I eat by reading my article "The Size Diet" in Sci-Tec Nutrition's "Reform" magazine (debut issue, which appeared at the Arnold).

You may also find value in my Glucose Economy (TM) concept, discussed in extensive detail in ProLab's "No Mistakes Nutritional Guide", available at places like Nutros.com, **************, and at GNCs soon.

Thanks, Jonathan, for your attention.

Best,
Robert Thoburn

[robertthoburn]

You can also see it advertised in Muscular Development, Flex, Planet Muscle.