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WHAT EXACTLY ARE AMINO ACIDS? AND HOW YOUR BODY USE THEM??

Amino Acids are one of six basic nutrients your body needs.

Proteins, vitamins, minerals, carbohydrates, fats and water are the basic nutrients your body needs and uses every day. Take the water and fat out of your body , and proteins are approximately 75 % of whats left. Muscle fiber, cell membranes, enzymes, the neuro-chemicals that make your brain run - are all proteins. Your body needs thousands of complex proteins to run every second. And, your body constantly builds these new proteins from isolated, singular Amino Acids. Your body must first digest its protein food sources, such as eggs, milk, meat or rice and beans into amino acids and then it rebuilds the amino acids back into proteins, body proteins.

Isolated amino acids are the key to protein metabolism

Are amino acids supplements for you?

How are isolated amino acids made?

Since your body cannot directly use proteins found in food sources, it digests, or catabolizes, food proteins into isolated singular amino-acids. As found in dairy, animal, tofu or any other food source, proteins consist of chains of hundreds, or even thousands , of amino acids, joined with peptide bonds. Your body uses an array of precision biochemical tools, including dozens of enzymes, to break all of these peptide bonds and create isolated-singular amino acids.

Then your body recombines, or anabolizes, these isolated-singular amino acids into proteins. Your protein metabolism uses 8 or more specific isolated-singular amino acids to create 150 or more other intermediates inside the body and the more than 40,000 proteins known so far to science. Your body can’t store amino acids, and will break down it’s own protein structures, including healthy muscle, to meet its need for isolated-singular amino acids.

“Pre-digested” proteins, protein isolates or peptide-bonded amino acids (which are all basically the same thing as predigested proteins) such as whey, casein, lactalbumin, albumin (these are milk and egg proteins) and soy are often suggested to supplement amino acids metabolism. These are food proteins chemically treated to break some, but not all, of the peptide bonds. “Predigested” proteins still contain chains of hundreds or thousands of peptide bonded amino acid proteins. So your body still has to digest them.

FOOD PROTEINS

PRE-DIGESTED PROTEIN, PROTEIN ISOLATES & PEPTIDE BOND

ISOLATED SINGULAR AMINO ACID

These protein sources will also have the food characteristics and allergy potential of the original protein source, whether it be animal byproducts, dairy, or egg. The Chemical processing in pre-digestion is not nearly as discriminating as the body’s own digestive mechanisms, and will often make the resulting amino chain more difficult, or even impossible, to digest.

Food protein sources and even high-quality “predigested” and peptide bonded proteins can provide an adequate protein intake. It’s still fairly difficult, however to achieve just the right balance of amino acids for your body’s specific metabolic needs. An imbalanced diet, stress, and drug use can all contribute to an unbalanced amino acid metabolism. What’s more, specific imbalances can be caused by particular lifestyles.

Weight lifters and the physically active may require more of the branch chain amino acids L-Leucine, L-Isoleucine, L-Valine, which play a key role in muscle mass development. Sulphur amino acids, found in high quantities in garlic, are powerful detoxifiers. Glycogenic amino acids help regulate your glucose metabolism and play a key role in managing blood sugar levels. L-Glutamine, L-Tyrosine, and L-Phenylalanine are central components of healthy neurotransmitter activity. And those with viral infections face a whole host of demands for isolated-singular amino acids form their immune systems.

Although your body can make 150 or more intermediates and 40,000 + proteins from the 8 or more essential, isolated amino acids, it can only make as much as allowed by the essential amino acid you have the least of. This ceiling, called rate limiting, makes balancing amino acid metabolism using food source proteins, predigested protein, protein isolates or peptide bonded proteins even more difficult. The difficulty in balancing food source proteins means that just about anyone, from weight lifers to weekend jocks, vegetarians to drinkers, the stressed out to the hypoglycemic, can benefit from isolated-singular amino acids supplements formulated for specific metabolic needs.

Isolated, singular L-crystalline amino acids are natural organic crystals grown naturally by a special fermentation process, which is similar to the process used to make tofu, yogurt, blue cheese and many other foods as well as most vitamins. Unlike peptide bonded amino acids, protein powders and liquids, isolated singular amino acids require no digestion, contain no allergenic protein fragments, are free of animal by products and can be combined to form precise amino acid formulations.

What to look for and How to take amino acids??

CONCLUSIONS

REFERENCES

If you want a true amino acid product look for USP/FCC pharmaceutical grade isolated, singular L-crystalline amino acids. (For best results always use encapsulated powder or powder form) Because isolated, singular amino acids require no digestion, use them 30 minutes before meals, between meals or before exercise or as direct by a physician.

Isolated singular amino acids play the key role in protein metabolism, and since your body’s solids, excluding fat, are approximately 75% protein, a critical role in overall health. A variety of lifestyles and conditions can indicate an imbalanced protein metabolism, and the need for amino acid supplements. “Predigested” or peptide-bonded amino acids must be further digested and retain any allergic food source characteristics. Isolated singular amino acids not only offer no digestion and no food source characteristics, but can be formulated to meet a variety of specific metabolic needs.

1. Styer L. Biochemistry (3rd ed). New York WH Freeman, 1988.
2. Conciee Encylopedia of Biochemistry, New York: Walter de Gruyter, 1983.
3. Munro HN, Crim MC. In Shils ME, Young VR (eds). Modern Nurtition in Health and Disease (6th ed). Philadelphia: Lea & Philadelphia: Lea & Febiger, 1988. Pp 1-37.
4. Stedman’s Medical Dictionary (23rd ed). Baltimore: Williams & Wilkinss, 1976.
5. Forbes GB. In Shils ME, Young VR (eds). Modern Nurtition in Health and Disease (7th ed). Philadelphia: Lea & Febiger, 1988. PP 533-556
6. Wannemacher Jr. RW In Ghadimi H (ed). Total Parenteral Nutrition. Premises and Promises, New York: John Wiley Sons, 1975. Pp 85-153.
7. Wannemacher Jr. RW, Owanda MC, Pekarek RS, et al. Infect Immun. 1971: 4:556.
8. McMurray gentlemen. Organic Chemistry Monterey, CA: Brooke/Cole. 1984.
9. Laidlaw SA, Kopple JD. Am J. Clin. Nutrition. 1987; 46:593-605.
10. Keith RE, JAMA. 1986; 255(9):1137.
11. Ehrenprels sincerely. Subet Alcoh Actions/Mieuse. 1982:3:231-239.
12. Walsh NE, Ramamurhy S.Schoenfield L, et al. Arch Phys Med Rehabil. 1986;67;4389.
13. Chipponi JK, Bleier JC, Santi MT, et al. Am J. Clin Nutr. 1983; 35;112-1116.
14. Visek WJ. Ann Rev Nutr. 1984;4:137-155.
15. Rodwell VW. In Martin Jr, DW et al (eds). Harper’s Review of Biochemistry (20th ed). Los Altos, CA: Lange, 1985; pp. 293318.
16. Tschudy DP, Bacchus H, Weissman S, et al. J. Clin invest. 1959; 38:892..
17. Bergstrom J,Furst P, Noree LO, et al. J. Appl Physiol. 1974; 36 (6):6937.
18. Jefferson LS, Flaim KE. In Blackburn GL, Grant JP, Young VR (eds). Amino Acids: Metabolism and Medical Application, Boston: John Wright, 1983. Pp 167-182.
19. Abumrad NN, Cersosimo E, Lacy WW. In Adibi SA, et al, (eds). Branched Chain Amino and Keto Acids in Health And Disease, New York: Krager, 1983. Pp. 162-181.
20. Scriver CR, Rosenberg LE. Amino Acid Metabolism and its Disorders, Philadelphia: WB Saunders, 1973.
21. Furst P. In Adibl SA, et al (eds). Branched Chain Amino and Keto Acids in Health and Disease, New York: Karger,1984. Pp. 268-278.
22. Traister J.Unpublished data. Presented at 21st Annual Meeting of The American Academy of EnviromentalMedicine, Clearwater Beach, Florida, October, 1986.
23. Bernstein LH. Am Clin Lab. 1989; 6-7.
24. O’Keefe SJD, Sender PM, James WPT. Lancer. 1974; 2:10358.
25. Long CL, Birkhahn R. Gelger JW, et al. Metabolism. 1981; 30(8):76576.
26. Thomas MF, Munto HM, Young VR. Biochem J.1979;178:139.
27. Minisola S,Antonelli R, Mazuoil G.J Clin Chem Clin Biochem. 1985;23:5159.
28. Moller SE, Larsen OB. In Usdin E. Et al (eds). Frontiers in Biochemical and Pharmacological Research in Depression, New York; Raven Press, 1984. pp.3196.
29. Krause MV, Mahun LK. Food, Nutrition and Diet Therapy (7th ed). Philadelphia: WB Saunders, 1984.
30. Goldberg AL, Odessey R. Am J.Physiol. 1984;223:1384.
31. Harper AE. Amer J.Clin Nutr. 1988: 21(5):358-368.
32. Silk DBA, Dawson AM. In Crane RK (ed). International Review of Physiology: Gastrointestinal Physiology III (Vol. 19). Baltimore: University Park Press, 1979. Pp.151-204.
33. Pardridge WM. Nut Rev. May 1986; Suppl: 15-25.

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