ganzo2

[3DC]

[3DC]

Re: ganzo2

Whey vs. Casein, that's my final answer.

Currently there has been debate of which protein is better for muscle building caseinate or whey? Recently an article has been written about the benefits of casein over whey. But a supplement company wrote the article so of course they leaned towards caseinate as the better of the two. But if you were to head over to another supplement company you would find the opposite story. Is caseinate the better protein for lean muscle growth because of slower digestion? Is whey the better protein because of faster digestion? What better place to come for that answer then Proteinfactory.com. As you might have already known, the protein factory reveals the truths behind the protein business. We are never biased to a certain protein because we offer every protein available on the planet. Now once and for all you will learn the answer; which is a better protein, whey or casein?
To answer this question we searched for articles written over the years describing the benefits of casein and whey. At the end of reading each article (which might take you a few days) you will have a clear picture of casein and whey.

The Ideal Form of Protein
By Luke R. Bucci, Ph.D., CCN C (ASCP) CNS.
It has been said that during the last decade science has revealed more sports nutrition breakthroughs than in the previous 100 years. For athletes in the know, this is their secret weapon, the place where brains and brawn come together to go beyond genetic potential. This article will focus on the state of the art for protein, the most revered macronutrient for athletic recovery and growth.

What Forms of Protein Intake are Available?

Whole Food Proteins: The oldest method for getting your daily dose of protein comes from Mother Nature. The protein sources in this group are supplied from intact or whole foods such as meat, fish, poultry, dairy products or vegetables. Not so long ago this was the only way to get protein into our diets until the advent of protein supplements, which are now readily available.

Protein Supplements: These supplements contain purified forms of native proteins such as Whey, Egg or Soy, with the degree of purification being quite different from product to product. The varying degrees of purification go from protein concentrates (lower grade) to isolates, which are much higher in quality. In any case most protein supplements are usually low in fat and add only moderate amounts of carbohydrate, a welcome feature for athletes who want to stay lean.

Free Form Amino Acids: Due to their unique properties, the use of pharmaceutical grade (pure and sterile) free form amino acids to support muscle repair and growth would work best by being injected into the bloodstream. Feeding people this way is called parental feeding, or total parental nutrition (TPN). TPN was a great medical advances because it feeds people whom otherwise could not eat. Most of the scientific research done on free amino acids has revealed that they work best taken on an empty stomach. When free amino acids are taken without interference from other proteins they can be utilized to elicit specific responses.

Protein Hydrolysates: Protein can be hydrolyzed (broken into smaller pieces) by enzymes, producing small chains of amino acids called peptides. This process mimics our own digestive actions thus making it an ideal way to process protein. Keep in mind that protein quality must always be considered regardless of which form is ingested. Also, one can mix all of the forms together in unlimited ways. Table One gives some pros and cons for each form of getting amino acids into the bloodstream.

Step One: How is Protein Absorbed, Really?

Scientists and doctors realized in the late 60s and early 70s that protein is not completely broken down to single (free) amino acids inside the small intestine (gut), and then the single amino acids absorbed by the gut and simply transferred to the bloodstream. Rather, proteins are chopped into small pieces in the stomach and gut by acid and enzymes. When the pieces get between four and six amino acids long (small Oligopeptides), enzymes on the surface of gut cells quickly chop them up into even smaller peptides (either two or three amino acids long) and single amino acids. These little pieces (one, two or three amino acids long) are taken inside gut cells. Anything larger simply does not get into gut cells in significant amounts. The pieces that are two amino acids long (di-peptides) and three amino acids long (tri-peptides) are then chopped into single amino acids inside the gut cells by hordes of enzymes. Chopping di- and tri-peptides into single amino acids is practically instantaneous after being taken up into gut cells. The single amino acids are then rapidly dumped into the bloodstream.

The Magic of Small Peptides
Why would our gut want to absorb di- and tri-peptides instead of single amino acids? The answer is easy - economy of effort. To absorb anything from inside the intestine to the inside of gut cells, membranes must be crossed. This means receptors must be used to take in substances into gut cells. Gut cells are loaded with receptors that grab nutrients very selectively. No receptor, no absorption. Gut cells have receptors for single amino acids, but they have even more receptors for di-peptides and tri-peptides.

Receptors are like subway turnstiles - only one molecule at a time can pass through. Because di-and tri-peptides are small enough to pass through receptors as fast as single amino acids, our bodies have figured out that by absorbing a tri-peptide, it can get three amino acids for the cost of one. It is then very easy to have lots of peptidase enzymes inside the gut cells that rapidly chop the tripeptide into single amino acids, which are pushed out of intestinal cells into the bloodstream as single amino acids. Cells throughout the body (especially muscle cells) can then pick and choose what single amino acids they want.
This means that instead of having a bunch of single amino acids queuing up to go through a limited number of intestinal turnstiles, di- and tri-peptides push through two or three people at a time. The net result is 2-3 times more people (amino acids) on the subway (bloodstream) in the same time period as if people went through the turnstiles one at a time. Efficiency is the key.

Evidence For Taster Absorption of Amino Acids
From Peptides - Peptides Versus Intact Proteins

Is there any evidence that hydrolysated (peptides) are better than food proteins or intact proteins for getting amino acids into the bloodstream? Yes, so much so that it is now considered dogma. Hospitals routinely use hydrolysate products from pharmaceutical companies as the primary amino acid source for feeding patients in hospitals. A large and consistent body of literature has shown that at higher levels of total amino acid intake (obviously bodybuilders are at the high end) hydrolysates are absorbed faster than either intact proteins or free form amino acids. Usually hydrolysates get into the bloodstream about twice as fast as intact proteins or free form amino acid mixtures in normal humans. This coincides perfectly with the subway turnstile analogy.

Let's skip the animal and hospitalized human studies, and look at research that more closely applies to bodybuilders. Ten years ago, Grimble and coworkers from the Department of Gastroenterology and nutrition in Central Middlesex Hospital in London, United Kingdom, looked at absorption of amino acids from intact egg protein and different degrees of hydrolysis in 12 normal humans. Best uptake came from the hydrolysates richest in di-and tri-peptides. These results clearly show that a small peptide hydrolysate is preferred to a partial hydrolysate or intact protein for getting amino acids into the bloodstream faster in humans.

A recent study by Collin-Vidal from the Human Nutrition Laboratory of the University of Clermont at Auvergne in France fed 12 normal volunteers either carbohydrates / lipids alone or with whole casein or casein peptides continuously by a nasogastric tube. Leucine metabolism was measured as a marker of protein metabolism by a leucine tracer. Similar to bodybuilders, these subjects were in positive leucine balance and were already eating a high intake of leucine. Subjects showed higher leucine levels in the bloodstream; more protein synthesis and more leucine oxidation with the hydrolysate, indicating more leucine got into muscles and other tissues. Since the subjects were not exercising, extra leucine was broken down (oxidized for energy) instead of being used to build muscle. The moral of the story is that if these subjects were exercising, then more of the leucine would have been targeted to building muscle and not broken down. The net result is that more leucine got to tissues (including muscles) with the hydrolysate.

An overwhelming amount of literature has reported the superiority of hydrolysates over equivalent compositions of free form amino acids for getting amino acids into the bloodstream faster. As an example, a report by Silk from Middlesex Hospital in London using normal humans will be examined. First, absorption of amino acids was greater from hydrolysates of casein or lactalbumin (whey) than from equivalent free form amino acid mixtures. In fact 11 out of 16 amino acids measured where absorbed significantly better, including leucine, valine and glutamine. In fact, glutamine absorption was doubled by hydrolysates.

Sergio!!
in Italian please

[3DC]

Re: Re: ganzo2

Another important point is that hydrolysates can get more amino acids into the bloodstream faster into normal, healthy volunteers than an equivalent free form amino acid mixture when intakes are high. What does this mean in real life? According to a study by Hegarty from St. Bartholomew’s hospital in London, England, whey protein hydrolysate (lactalbumin) and an identical composition of free form amino acids were equivalent in uptake until 12 grams of total amino acids were given. Over 12 grams of intake, uptake of every amino acid from the hydrolysate was equal to or superior to the free form amino acid mixture. Again, a doubling of glutamine uptake was found. This is very important for bodybuilders, because 12 grams is a measly amount of amino acids compared to typical intakes of 50 grams of amino acids per meal. Thus, at high intakes of protein, hydrolysates get absorbed better than intact proteins or free form amino acid mixtures.

It is easy to relate these results to real life. Free form amino acid receptors on gut cells can keep up with peptide receptors until a certain level of total amino acids are reached (about 12 grams per feeding), then the subway turnstile effect comes into play for hydrolysates, showing their superiority for amino acid absorption at real-life levels of supplementation.

Why is Faster Amino Acid Absorption Better for Bodybuilders?
Why all the fuss about getting more amino acids into the bloodstream faster? The answer is simple - more amino acids in the bloodstream (especially with insulin) means more amino acids in muscle means more muscle protein synthesis means more growth/recovery/repair.

We already know that protein needs of weightlifters are double those of other athletes and sedentary people. We also know that after lifting weights, amino acid transports protein synthesis and protein breakdowns (catabolism) are all increased in muscles. We also know that amino acids, not carbohydrates, fat or insulin, are responsible for increased anabolism (more protein synthesis and less protein breakdown) in humans after eating. In other words, muscles are hungry for amino acids, which they can only get from the bloodstream, right after a workout (within 30 minutes). This happens to be the window where hydrolysates are superior to proteins or free form amino acid mixtures.

Before we get too focused on protein, keep in mind that right after a weight-training workout; a combination of protein and carbohydrate outperformed both protein alone and carbohydrate alone for increasing insulin and growth hormone levels. Thus, even an ideal hydrolysate would have better effects when consumed with simple carbohydrates since carbohydrates are absorbed by different receptors on gut cells, there is little or no competition with amino acids and peptides for absorption.

Whey vs. Casein: Hyperaminoacidemia: the Anabolic Edge By Michael Gundill

Until now, proteins have been viewed from a quantitative aspect because they were considered inert and inactive. It’s time to reconsider the view: Proteins contain amino acids that are indeed powerful growth factors. You can only obtain the muscle building effect of proteins with qualitative approach, something that bodybuilders have neglected. What really matters is the number of feedings, the proper times and the dynamic manipulation of both the amount and the source of proteins. I’m going to show you how to take advantage of the pharmaceutical muscle-building effects of proteins.

Fast, Anabolic Proteins vs. Slow Anti-catabolic Ones

Whey and Casein are very closely related forms of proteins that are both derived from milk. Bodybuilders used to consider them interchangeable. Some argued that whey was superior to casein, while others claimed the opposite. As a result bodybuilders used either whey or casein but not both, with each camp thinking that it had found the very best protein. Whey and casein have two radically different but complementary muscle-building properties. Indeed, a recently published French study compared those properties and the results showed that oral intake of 30 grams of whey protein very rapidly increased the level of amino acids in the blood in healthy young subjects. Consequently, anabolism was boosted by 68 percent.

Unfortunately whey’s muscle-building potential is transient-the paired and important rise in blood amino acid level is followed by a quick fall-and the results also showed no significance anti-catabolic effects.

On the other hand, 30 grams of casein resulted in a delayed but long-lasting elevation of amino acid levels in the blood, while the anabolic boosting effect were 31 percent milder than those of whey. In fact, casein’s long-lasting, anti-catabolic effect was its main advantage.

Since whey and casein are very different, you should use whey whenever you want a strong and rapid boost of anabolism. It’s a superior protein to eat first thing in the morning and immediately after training. Casein is the best choice whenever you need long lasting anti-catabolic protection: for example at night.

Note that the qualities of being anabolic or anti-catabolic apply to more than skeletal muscles. The researchers measured both whole body protein synthesis and degradation, so we don’t know exactly how much the muscles have benefited from those favorable effects. Nevertheless, its obvious that muscle growth is faster in an anabolic or anti-catabolic environment than in a strongly catabolic situation. As the study involved untrained subjects, its likely that bodybuilders would have gotten even stronger effects because of their protein-hungry muscles.
This study demonstrates the importance of timing protein intake and choosing the right source of protein. The results bring us to another fundamental question" Why is whey so anabolic when casein is so anti-catabolic?

Blood levels of amino acids do not fluctuate that much during the day in healthy bodybuilders. Eating a meal rich in proteins elevates the amino acids level slightly but not much. Fasting during the night slightly reduces it. In that case catabolic hormones such as cortisol will rise and induce muscle proteolysis; that is the breakdown of protein. Some of the muscle’s amino acids will therefore pass into the blood, which helps sustain a constant blood amino acid level while you sleep. Consequently, blood amino acid levels are never very high or very low for very long-unless you fast for a prolonged period.

The term hyperglycemia means there’s too much glucose in the blood. You may be more familiar with the rem hypoglycemia, which describes a low blood glucose level. As with the blood amino acid level, glucose is closely controlled. Glycemia may rise after a high carb meal, but unless you suffer from diabetes, it will be brief and moderate. When you fast, your blood glucose level falls slightly. That triggers the manufacture of glucose from amino acids in both the liver and the kidneys, which boosts blood glucose levels. As a result your blood glucose levels are also never very high and never very low.

Similar to the terminology used for glucose, Hyperaminoacidemia occurs when blood amino levels are greatly increased, and Hypoaminoacidemia occurs when they are low. The key point for bodybuilders is that a Hyperaminoacidemia induced by an amino acid intake automatically triggers anabolism. Scientists have discovered that there are thresholds of amino acids in the blood: When you get past a certain level of elevation anabolism is triggered. As you can imagine, its no that easy to reach the threshold. Scientists use amino acid infusion.

As stated above, ven a meal that’s is rich in protein s is unlikely to induce a significant Hyperaminoacidemia. Proteins from foods are slow to digest, so their arrival in the blood is sustained but very slow, and consequently, the amino acid level in the blood rises slowly. Once is slightly elevated organs such as the liver remove those aminos from the blood. As they enter the blood slowly, the liver has no trouble keeping up. So the rise in blood amino acids is never as high as bodybuilders might wish. In contrast, the amino acids infusions given by scientists bypass the digestive track, and the level. Of blood amino acids increases quickly, which overwhelms the liver’s ability to extract amino acids from the blood, creating a condition of Hyperaminoacidemia. Growth is triggered by pharmacological means.

Until recently, it was almost impossible to induce a pharmacological Hyperaminoacidemia with food or supplements, so bodybuilders had to make do with more moderate physiological Hyperaminoacidemia. That’s a shame, as the stronger the Hyperaminoacidemia, the more powerful the anabolic drive. The arrival of predigested whey protein was a big breakthrough for the bodybuilding community, as it has the amazing property of inducing a quick sharp elevation of the amino acid level in the blood. In other words, it can trigger the strongest Hyperaminoacidemia possible.

By almost bypassing digestion, whey protein overwhelms the liver capacity for extracting amino acids from the blood. It affects your body in a pharmacological way that only amino acid infusion can duplicate.

That is not possible with casein. Its is slow digestion only products a physiological Hyperaminoacidemia, which means the amino acid level is high but within normal limits.
Meals rich in protein wont induce a pharmacological Hyperaminoacidemia, either as the digestion of protein is even slower than what occurs with casein because of the fibers, fats and other elements that delay digestion.

[3DC]

Re: Re: Re: ganzo2

Long-Term Muscle Protection Against Catabolism
As the amount of whey you eat at a given time is limited, the fast and powerful arrival of amino acids is short-lived. When new amino acids stop arriving in the blood, the organs that extract them stop being overwhelmed and the blood levels of amino acids are brought back to normal. When that happens, the powerful effects of whey vanish. Anabolism falls and catabolism dominates again.
Casein does not produce such a rise and fall in blood amino acid levels due to its timed-release action. The blood level of amino acid s elevates slightly but for a long period. Scientists have shown that a small elevation of blood amino acids greatly reduces catabolism. You could get a long-lasting anti-catabolic effect like that with whey if, instead of absorbing 30 grams at once, you took 10 grams every hour. You would not get any pharmacological Hyperaminoacidemia, but the constant arrival of small amounts of amino acids would reduce catabolism.
By the same token, if the researchers in the French study had used 60 grams of casein instead of 30, its more likely that the subjects blood amino levels would have reached the critical threshold at some point. In that case casein, after a delay, would have first reduced catabolism, and then, when the peak of blood amino acids had been reached, it would have triggered anabolism. After that peak the casein would have recovered its mainly anti-catabolic function and stopped being significantly anabolic.
There are three points to remember from this study.
1. Whatever the dose is, amino acid derived from whey will always reach the blood before the amino acids derived from casein.
2. The long-lasting anti-catabolic effect of casein can be duplicated by frequent ingestion of small amounts of whey. Of course its unlikely that you’re going to wake up every hours during the night to have your whey drink, so whey proteins are not’t practical if you’re looking for a prolong anti-catabolic effect.
3. In order to get a strong anabolic action from casein, you need a far higher dose of it than whey to get the same effect-and casein’s effect take a lot longer to kick in than whey’s effects.

Comments


ANABOLIC
The most important fact in the article HYPERAMINOACIDEMIA. With the use of a hydrolyzed whey protein you can achieve this effect. Getting a flush of amino acids into the blood stream will cause an anabolic effect. Using regular whey protein concentrate or whey isolate will not do this. But what the article failed to do was to go into detail about hydrolyzed whey protein. If you want details about hydrolyzed whey protein, read article #2 Hydrolyzed whey protein and their friend the peptide. Only the proteinfactory.com offers the lowest MW hydrolyzed whey protein the 520. But I won’t take credit for the first company to do this. back in 1998. Metaform put out a supplement called Proton. It contains hydrolyzed whey and hydrolyzed casein. Great supplement but contained fructose and of course tasted like horses’ ass. Thus it did not sell. They also had a tit for tat with AST research a while back. AST tried to claim their protein was hydrolyzed whey but no –no total scam. If you have not learned yet- HYDROLYZED PROTEIN TASTES TERRIBLE EVEN IF YOU ADD FLAVORING.

ANTI-CATABOLIC
Only casein can provide this effect. But you have to make sure you taking enough do to this. If you’re going to try to get the anti-catabolic effect from casein.

Conclusion
Timing is everything. Select your proteins carefully and use them at the proper times. Use whey proteins in the mornings and after workouts. Use casein with MRP's and protein powders during the day. Each protein, just like soy, egg, milk, and bovine all have their special properties. If you use them at the right times you will maximize their use.

[JOBLACK]

The pen is on the table.
And the table is browne.


Non mi sarei messo a leggere dta pappardella neanche in italiano, figurati in inglese

[3DC]

READ THIS

HELLO

[polpy]

Re: READ THIS

Originally posted by 3DC
HELLO

HI!

ken iou tradus ior article in italian ?

[vance]

noio volevan savuar l'idiriss dela chesa...........

[polpy]

Re: Re: Re: Re: ganzo2

Originally posted by 3DC

ANTI-CATABOLIC
Only casein can provide this effect. But you have to make sure you taking enough do to this. If you’re going to try to get the anti-catabolic effect from casein.

Conclusion
Timing is everything. Select your proteins carefully and use them at the proper times. Use whey proteins in the mornings and after workouts. Use casein with MRP's and protein powders during the day. Each protein, just like soy, egg, milk, and bovine all have their special properties. If you use them at the right times you will maximize their use.

Interessante, ma... sarà vero?