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Answer: Simply put, probiotic organisms are the friendly bacteria that we should all have in our intestines to help us break down the food we eat and to assist with nutrient absorption. On the average, a human being carries around approximately 4 pounds of bacteria in the intestinal tract. Ideally, our intestines should contain the maximum percentages of probiotic, friendly bacteria and low levels of bad bacteria, such as yeast, mold, and staph. organisms. In actual fact, however, the bad organisms outnumber the probiotic organisms in our intestines, and this skewed ratio can lead to health and digestive disorders. We can start to change the ratio of friendly to bad bacteria in our intestines by regularly consuming live (viable) friendly bacteria in the foods we eat. With a regular regimen of viable probiotic organism consumption, studies have shown that the numbers of friendly bacteria in the intestines will rise and the numbers of bad bacteria will correspondingly decrease. The result is a healthier intestinal tract, increased efficiency of food digestion, and increased nutrient absorption.
Some recent studies have suggested that probiotic organisms can actually be of extra benefit to people who follow extreme diet regimens, such as people who consume high protein diets. When large quantities of protein are consumed, the body metabolizes the protein and produces nitrogenous compounds as a by-product of protein metabolism. These nitrogen containing compounds find their way back to the intestines, where, it is theorized, that the probiotic bacteria scavenge the nitrogen, manufacture new amino acids from the pool of compounds in the intestines, and then make these amino acids available for absorption back into the bloodstream. As the theory goes, the probiotic bacteria not only clean up the intestines, but also utilize the junk to make new, utilizable amino acids.
We culture the milk protein in our products with important probiotic organisms Bifidus, acidophilus, and yogurt culture organisms. They are all classified as probiotic organisms. The health benefits of yogurt organisms have been well documented over many years. Bifidus organisms not only help our digestive/absorption process but they also synthesize the important Vitamins B and K, which our bodies can then absorb for our own use. Acidophilus assists in digestion of carbohydrates and proteins by manufacturing enzymes to help break them down into smaller pieces for easier absorption. These organisms are viable and available to assist your digestive processes when you consume our protein powders.
What are prebiotics? Prebiotics are the "food" that probiotic organisms live on. We add prebiotics to every serving of Pro MR to help grow the probiotic organisms and to allow them to make their valuable contribution to your overall well being.
Answer: To answer that, we first have to explain a little bit about the science behind our products. Basically, through the sound, scientific principles of "Fast and Slow Dietary Proteins", research has concluded that no single source protein supplement is the ideal method to grow new muscle tissue (anabolism) while, at the same time, preventing muscle tissue breakdown in the body (catabolism). If one consumes only Fast proteins, the amino acids enter the bloodstream too fast, stimulating protein synthesis, but also causing the body to divert a significant percentage of the amino acids to the liver, where they are oxidized and used for energy instead of for promoting lean tissue growth. If you combine quality proteins with differing digestion rates in the correct ratios, you can eliminate this uneconomical scenario by creating a sustained release effect. We have combined different types of Fast proteins, in the form of whey protein concentrate, isolate, hydrolysate, and egg white, with a Slow protein source, micellar casein. With this combination of Fast and Slow Dietary Proteins we are trying to ensure that precise amounts of amino acids will be released into the system at exactly the right times, so as to maintain a constant positive nitrogen balance and an ideal anabolic / anti-catabolic environment for muscle tissue development. You see, Fast proteins have been shown to be anabolic, but research has shown that certain fast proteins, such as whey proteins, have no anti-catabolic activity. On the other hand, a recent study concluded that micellar casein does have significant anti-catabolic activity by preventing protein breakdown in the body. For anybody who is serious about making lean tissue gains, a mixture of Fast and Slow Dietary Proteins is the only regimen to consider.
Answer: Nothing is wrong with whey protein. Whey protein is a highly nutritional, immune supporting protein source. Scoring systems that compare textbook profiles of protein sources consistently score whey protein very high. However, it is important to keep in mind that most commercially available whey proteins fall well short of the textbook profiles that score so high. You have heard it before, Not All Whey Proteins Are Created Equal! The most bioactive (anabolic) parts of whey proteins are also the most easily destroyed during whey protein manufacture. Almost every commercially available whey protein (including those in your favorite supplement powder) has been heavily processed, including heat treatments and pH changes. Both heat and pH adjustments will destroy the fragile, bioactive components of whey protein as well as degrade some of the more important amino acids that are claimed in support of whey proteins. Immunoglobulins and BSA start to denature (degrade) at temperatures as low as 140 degrees F. Most commercial whey proteins have been pasteurized at 170 degrees F. The standard whey protein has undergone much denaturation (degradation) and does not compare to the textbook profiles or scores for whey protein. Don't be fooled by whey protein supplement labels that claim specific protein fraction or amino acid compositions! The truth is that whey protein processing destroys portions of these protein fractions and amino acids! A standard whey protein can vary by as much as 15% in amino acid content from production batch to production batch and the protein fraction composition varies widely throughout the industry, depending on the manufacturing technique employed during production. Most commercially available whey proteins are significantly different from whey protein textbook descriptions in important nutritional properties. Given the differences between textbook compositions and real world whey proteins, it is not valid science to make claims for real world whey proteins based on textbook studies.
It is also important to keep in mind that while whey proteins have been shown to be anabolic, due to their immuno-supportive, bactericidal, and antiviral functions, a recent study concluded that whey proteins have no effect on protein breakdown in the body (no anti-catabolic function). While anabolic performance is important, you need your protein diet to have some anti-catabolic function for maximum lean tissue growth.
Answer: Whey proteins have nutritional properties that extend well beyond protein quality as measured by amino acid composition. Whey protein contains components known as protein fractions and peptides that have been shown to have bioactive properties. These bioactive properties may be the most nutritionally effective components of whey protein. As we have already stated, standard industry processing procedures significantly reduce the bioactive functions of whey protein. Most of the reference studies quoted by the leading marketers of whey protein supplements in their advertisements were performed using special, custom manufactured whey proteins and do not correspond to standard, commercially available whey proteins. G. Bounous, in a study that is frequently quoted in whey protein magazine ads, made his own Whey Protein X in a university laboratory by a special, low heat process. In the Bounous study, Protein X was compared to commercially available sources of whey proteins and was found to be significantly superior to standard whey proteins in all categories. Bounous actually concluded that Protein X was far superior to the commercial brands that were used for comparison. Yet, clever whey protein marketers love to quote the Bounous study when attempting to convince you that their whey protein has such great benefits. The Bounous study showed that not all whey protein is as good as the textbook claims. It is interesting then that so many whey protein marketers quote the Bounous study when it convincingly showed that commercially available whey proteins were not as good as textbook proteins.
We resolved to find a whey protein that lived up to the textbook claims and to studies such as Bounous. We searched the entire world for a whey protein manufactured under the most ideal conditions, only to find that it did not yet exist. Through our efforts, certain factories have agreed to manufacture a whey protein under processing conditions that we have specified. The result is a whey protein with the best possible whey protein fraction content and maximized bioactive properties. Our custom manufactured whey protein comes as close as possible to providing the quality of protein as presented in textbooks and the widely quoted reference studies on whey proteins.
Answer: Casein is hardly a poor quality protein. For many years, casein has been considered the standard reference protein by which all other protein qualities are measured and compared. In order to sell 100% whey protein powders, some unscrupulous companies have tried to convince consumers that casein is of poor quality - even going so far as to hint that casein may be dangerous. Casein is GRAS (generally regarded as safe) listed by the US FDA and is one of the few food components to achieve that status. Casein contains many bioactive peptide sequences that provide important benefits for the body. In fact, the highly regarded peptide, glycomacropeptide, which many people believe to be a whey protein, is, in reality, a peptide chain from casein that finds its way into cheese whey protein as a by-product of cheese manufacture. Think for yourself - human maternal milk contains 40% to 55% casein.
Our products contain micellar casein. Micellar casein differs from "caseinate" in that micellar casein is not denatured and is the naturally occurring form of casein. A recent study involving 16 healthy, well fed individuals compared the effects of whey protein to micellar casein on whole body protein utilization. This ground breaking study came to several important conclusions:
Micellar casein significantly inhibited protein breakdown (anti-catabolic function) over seven hours after ingestion. Whey protein had no effect on protein breakdown.
Micellar casein moderately stimulated protein synthesis (anabolic function).
Less amino acids were wasted through liver oxidation after micellar casein ingestion than after whey protein ingestion.
Micellar casein resulted in better overall nitrogen retention in the body compared to whey protein!
Micellar casein is anti-catabolic and is an important component in the sustained release of amino acids into the system for maximizing anabolism.
Answer: Good thinking, but there are two problems with that line of thought. In the first place, several studies have demonstrated that whey protein is a fast dietary protein. With a fast dietary protein, all that happens is that every time it is consumed, the amino acids are released quickly into the bloodstream in a large grouping. It is the fast, excessive release of amino acids that causes the body to send a significant portion of the aminos to the liver for oxidation. These same studies have shown that as each new batch of amino acids is released into the bloodstream in a large group so often, a lower percentage is used for lean tissue growth support and a higher percentage is oxidized in the liver. Even worse, these percentages become more skewed on each successive protein ingestion, resulting in a reduction in the efficiency of protein utilization. Why waste your money consuming whey protein more often when the benefits would be doubtful at best?
Secondly, the ground breaking study comparing micellar casein to whey protein concluded that micellar casein significantly inhibited protein breakdown and that whey protein had no effect on protein breakdown. It did not say that whey protein had a slight effect or somewhat of an effect on protein breakdown. The study concluded that whey protein had no effect on protein breakdown. In other words, you can eat all of the whey protein you want as often as you desire, but it will not have an anti-catabolic effect.
Answer: Egg white protein scores very high on all of the known protein scoring systems. Egg white is also among the lowest heat treated proteins available. Low heat treatment means low denaturation and better absorption. We have included egg white protein in our products because its short peptide chains enter the system very fast, thereby initiating our protein blend's "sustained release" action. Egg white also contains high levels of the important amino acid cysteine. On the average, egg white contains more cysteine than the standard whey protein. Recent studies have demonstrated that cysteine may play an important role in muscle tissue growth.
Answer: Glutamine is included in these types of formulations because it is well known that supplementing with glutamine can result in increased lean tissue growth. Recent studies have suggested that glutamine supplementation is effective because it provides an immediate boost in growth hormone and free testosterone levels. These same recent studies have also suggested that food, particularly proteins or other amino acids, may decrease glutamine's anabolic effect. L-glutamine is a free amino acid and, as such, can only be absorbed into the blood via a competitive absorption mechanism. It is this competitive absorption mechanism that may be responsible for the decreased anabolic effect of glutamine when the free amino acid is consumed in the presence of food, protein, or other amino acids.
On the other hand, there are numerous studies that have concluded that peptide bound amino acids are absorbed far more efficiently into the body than free amino acids. Some studies claim that peptide bound amino acids are absorbed up to 20 times better than free amino acids. We use only peptide bonded glutamine for our products because we are trying to ensure that you get the maximum anabolic benefits of glutamine. There is little evidence that supplementing a protein powder with L-glutamine is beneficial. There is, however, much evidence that peptide bonded amino acids are efficiently absorbed and that their benefits are then realized. It only makes sense that consuming L-glutamine in the presence of other proteins or amino acids is a waste of money. On the other hand, consuming peptide bonded glutamine in conjunction with other protein sources and amino acids will be of benefit.
Answer: When Dorian Yates set out to make his own line of premier protein powders and meal replacers, he wanted, above all else, to make sure that the products would contain the highest quality ingredients and would provide the maximum possible benefits. The proteins used in these products are among the most expensive in the world. They are custom manufactured to ensure maximum effect to our consumers. In this industry, you get what you pay for. We pay high prices for the best quality ingredients to provide you with the best, scientifically based protein powders. We do not pretend that these products are for everyone. Our powders are made for serious athletes. They were developed by a champion bodybuilder for athletes intending to perform at championship levels. Pro MR and ProPeptide are Made by a Champion for Champions!