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- Branched Chain Amino Acids
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Also known as: Branched chain,
BCAAs
What do they do? Branched-chain amino acids (BCAAs) include leucine, isoleucine, and
valine. BCAAs are essential to the human body. They are needed for the maintenance
of muscle tissue and appear to preserve muscle glycogen stores1
and help prevent muscle protein breakdown during exercise.2
Some research has shown that BCAA supplementation
(typically 1020 grams per day) does not result in meaningful changes in body
composition,3 nor does it improve exercise
performance 4 5
6 7 or enhance the effects of physical
training.8 9 However, BCAA
supplementation may be useful in special situations, such as preventing muscle loss at
high altitudes10 and prolonging endurance
performance in the heat.11 Studies by one group of
researchers suggest that BCAA supplementation may also improve exercise-induced declines
in some aspects of mental functioning.12 13 14
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BCAAs can active glutamate
dehydrogenasean enzyme that is deficient in amyotrophic lateral sclerosis (ALS),
also called Lou Gehrigs disease. In one double blind trial, 26 grams per day of BCAA
supplements helped those with ALS maintain muscle strength.15 However, a
larger study was ended early when people using BCAA not only failed to improve, but
experienced higher death rates than the placebo group.16 Other
studies have shown no benefit of BCAA supplementation for ALS or other neuromuscular
diseases.17 18
One study investigating the advantages
of BCAA supplementation for diabetics undergoing an intense exercise program found no
additional benefit of BCAA on reducing abdominal fat or improving glucose metabolism.19
Patients with liver diseases that lead to comacalled hepatic
encephalopathyhave low concentrations of BCAAs and excess levels of certain other
amino acids. Preliminary research suggested that individuals with this condition might be
helped by BCAAs. Double blind studies have produced somewhat inconsistent results,20
21 22 but a reanalysis of these studies found an overall benefit for
the symptoms of encephalopathy.23 Therapeutic effects of BCAAs have also been
shown in children with liver failure24 and adults with cirrhosis of the liver.25
Any treatment of people with liver failure requires the direction of a physician.People with chronic renal failure may also benefit from BCAA
supplementation.
A preliminary study found improved breathing and
sleep quality in people given intravenous BCAAs during kidney dialysis.26
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Product Recommendations |
- B.C.A.A
- 200 Tab
- As Low as $12.99
 
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600 mg. of Branched Chain Amino Acids that is needed to create a positive
nitrogen balance thus promoting muscular growth. |
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Pre Power
- 3 capsules provide: 1500 mg Inosine, 75 mg Ferulic acid, 1200 mg BCAA, 500
mg Cytochrome C, 1000 mg Calcium & Potassium Aspartate help boosts the efficiency of
oxygen usage in muscle cells, decrease lactic acid build-up for less burning and cramping
with faster recuperation.
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Phenylketonuria (PKU) is a genetic disease that
allows abnormally high amounts of phenylalanine and its end products to accumulate in the
blood, causing damage to the nervous system. A controlled trial demonstrated that regular
use of BCAAs by adolescents and young adults with PKU improved performance on some tests
of mental functioning.27
Where are they found? Dairy products and red meat contain the greatest amounts of BCAAs,
although they are present in all protein-containing foods. Whey protein and egg protein supplements are other sources
of BCAAs. BCAA supplements provide the amino acids leucine, isoleucine, and valine.
Who is likely to be
deficient? Only an individual deficient in protein
would become deficient in BCAAs, because most food sources of protein supply BCAAs. Few
people in Western societies are protein deficient.
How much is usually taken? Most diets provide an adequate amount of BCAA for most people,
which is about 2565 mg per pound of body weight.28 29
Athletes involved in intense training often take 5 grams of leucine, 4 grams of valine,
and 2 grams of isoleucine per day to prevent muscle loss and increase muscle gain, though
most research does not support this use of BCAAs.
Are there any side effects
or interactions? Side effects have not been reported with
the use of BCAAs, except in the one study of ALS described above. At high intakes, of
BCAAs are simply converted into other amino acids, used as energy, or converted to fat for
storage. However, individuals with kidney or liver disease should not consume high intakes
of amino acids without consulting their doctor.
At the time of writing, there were no well-known
drug interactions with branched-chain amino acids.
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- References:
- 1. Blomstrand E, Ek S, Newsholme EA. Influence of ingesting
a solution of branched-chain amino acids on plasma and muscle concentrations of amino
acids during prolonged submaximal exercise. Nutrition 1996;12:48590.
2. MacLean DA, Graham TE, Satlin B. Branched-chain amino acids augment ammonia metabolism
while attenuating protein breakdown during exercise. Am J Physiol 1994;267:E101022.
3. Kelly GS. Sports nutrition: A review of selected nutritional supplements for
bodybuilders and strength athletes. Med Rev 1997;2:184201.
4. Van Hall G, Raaymakers JSH, Saris WHM, Wagenmakers AJM. Supplementation with
branched-chain amino acids (BCAA) and tryptophan has no effect on performance during
prolonged exercise. Clin Sci 1994;87:52 [abstract #75].
5. Blomstrand E, Hassmen P, Ek S, et al. Influence of ingesting a solution of
branched-chain amino acids on perceived exertion during exercise. Acta Physiol Scand
1997;159:4149.
6. Van Hall G, Rasymakers JSH, Saris WHM, Wagenmakers AJM. Supplementation with
branched-chain amino acids (BCAA) and tryptophan has no effect on performance during
prolonged exercise. Clin Sci 1994;87:52 [abstract #75].
7. Madsen K, MacLean DA, Kiens B, et al. Effects of glucose, glucose plus branched-chain
amino acids, or placebo on bike performance over 100 km. J Appl Physiol 1996;81:264450.
8. Vukovich MD, Sharp RL, Kesl LD, et al. Effects of a low-dose amino acid supplement on
adaptations to cycling training in untrained individuals. Int J Sport Nutr
1997;7:298309.
9. Freyssenet D, Berthon P, Denis C, et al. Effect of a 6-week endurance training
programme and branched-chain amino acid supplementation on histomorphometric
characteristics of aged human muscle. Arch Physiol Biochem 1996;104:15762.
10. Schena F, Guerrini F, Tregnaghi P, et al. Branched-chain amino acid supplementation
during trekking at high altitude. The effects on loss of body mass, body composition, and
muscle power. Eur J Appl Physiol 1992;65:39498.
11. Mittleman KD, Ricci MR, Bailey SP. Branched-chain amino acids prolong exercise during
heat stress in men and women. Med Sci Sports Exerc 1998;30:8391.
12. Hassmén P, Blomstrand E, Ekblom B, Newshomle EA. Branched-chain amino acid
supplementation during 30-km competitive run: mood and cognitive performance. Nutrition
1994;10:40510.
13. Blomstrand E, Hassmen P, Ek S, et al. Influence of ingesting a solution of
branched-chain amino acids on perceived exertion during exercise. Acta Physiol Scand
1997;159:4149.
14. Blomstrand E, Hassmen P, Ekblom B, et al. Administration of branched-chain amino acids
during sustained exerciseeffects on performance and on plasma concentration of some amino
acids. Eur J Appl Physiol 1991;63:8388.
15. Plaitakis A, Smith J, Mandeli J, et al. Pilot trial of branched-chain amino acids in
amyotrophic lateral sclerosis. Lancet May 7, 1988:101518.
16. The Italian ALS Study Group. Branched-chain amino acids and amyotrophic lateral
sclerosis: a treatment failure? Neurology 1993;43:246670.
17. Tandan R, Bromberg MB, Forshew D, et al. A controlled trial of amino acid therapy in
amyotrophic lateral sclerosis: I. Clinical, functional, and maximum isometric torque data.
Neurology 1996;47:122026.
18. MacLean D, Vissing J, Vissing SF, Haller RG. Oral branched-chain amino acids do not
improve exercise capacity in McArdle disease. Neurology 1998;51:145659.
19. Mourier A, Gautier JF, De Kerviler E, et al. Mobilization of visceral adipose tissue
related to the improvement in insulin sensitivity in response to physical training in
NIDDM. Effects of branched-chain amino acid supplements. Diabetes Care
1997;20:38591.
20. Maddrey WC. Branched chain amino acid therapy in liver disease. J Am Coll Nutr 1985;4:63950
[review].
21. Wahren J, Denis J, Desurmont P, et al. Is intravenous administration of branched chain
amino acids effective in the treatment of hepatic encephalopathy? A multicenter study. Hepatology
1983;3(4):47580.
22. Egberts E-H, Schomerus H, Hamster W, Jürgens P. Branched chain amino acids in the
treatment of latent portosystemic encephalopathy. Gastroenterol
1985;88:88795.
23. Naylor CD, ORourke K, Detsky AS, et al. Parenteral nutrition with branched-chain
amino acids in hepatic encephalopathy. A meta-analysis. Gastroenterology 1989;97:103342.
24. Chin SE, Sheperd RW, Thomas BJ, et al. Nutritional support in children with end-stage
liver disease: a randomized crossover trial of a branched-chain amino acid supplement. Am
J Clin Nutr 1992;56:15863.
25. Kato M, Miwa Y, Tajika M, et al. Preferential use of branched-chain amino acids as an
energy substrate in patients with liver cirrhosis. Internal Med
1998;37:42934.
26. Soreide E, Skeie B, Kirvela O, et al. Branched-chain amino acid in chronic renal
failure patients: respiratory and sleep effects. Kidney Int 1991;40:53943.
27. Berry HK, Brunner RL, Hunt MM, et al. Valine, isoleucine, and leucine. A new treatment
for phenylketonuria. Am J Dis Child 1990;144:53943.
28. Zello GA, Wykes LF, Ball RO, et al. Recent advances in methods of assessing dietary
amino acid requirements for adult humans. J Nutr 1995;125:290715.
29. Young VR, Bier DM, Pellett PL. A theoretical basis for increasing current estimates of
the amino acid requirements in adult man, with experimental support. Am J Clin Nutr
1989;50:8092.
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