New Member
I want to add an amino acid supplement product to aid my dieting and training. Could people with greater knowledge and experiance on them could recommend on something decent, what are the constiniuents and doses I should be looking for, rather than full of junk ingredients and poor incorrect dosages in which alot of products have.
Many thanks.
New Member
bump*
Associate Member
Hey man ... welcome to the board.
First of all amino acid supplements suck. stick to your protien shakes.... Wanna add something ?!! Try BCAA'S capsules of ON .. they're fine.
If you incist on amino acid supplements... go with the liqiud form ( not those horse pills ) .. try the amino fuel liquid by twinlab .. ( It tastes like shit but get over )...
If you want the horse pills ... try amino 2222 tabs by ON .. Take at least 15 ED
Good luck bro... Hope I helped you !!
AR-Hall of Famer
R U Serious? BCAA's are flippin' awesome - espcially when dieting. About 10 grams of the big 3 gets me wokin' up and immediatly stronger even when I am severely glycogen depleted...Originally Posted by BlackWidow
I like Optimum Nutritions line, I have used the caps many times but recently got a tub of the BCAA 5000 instanized powder... I am going to see how this stuff help pre-workout while bulking on a cycle. I love it while dieting/priming...
Here is some research on how it helps...
Enhance Strength -- Take Aminos Before and After Training
by Edmund R. Burke, Ph.D.
A study in the Italian journal, Medicina Dello Sport, investigated the effect of taking supplemental branched-chain amino acids (leucine, isoleucine, and valine) on bodybuilding progress. The study involved 31 male bodybuilders between ages 18 and 34, all of whom were drug free. All these athletes had at least two years of training experience, and were divided into two groups: 16 subjects ingested a placebo and 15 others ingested 0.2g per kilogram (2.2 pounds) of a branched-chain amino acid supplement 30 minutes before training and 30 minutes after the workout. The results showed that while bodyweight increased in both groups, those taking the BCAA supplement showed greater weight gains. Analysis of the composition of this weight increase in the BCAA group showed an increase in muscle mass in both the legs and arms, with no changes in the trunk area of the body. In contrast those taking the placebo showed no muscle mass gains in these areas. The BCAA group also showed strength gains in both the squat and bench press, while those ingesting the placebo got stronger only in the squat exercise.
Branched-chain amino acids and central fatigue.
Newsholme EA, Blomstrand E.
Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden. [email protected]
An account of the tryptophan (Trp)-5-hydroxytryptamine (5-HT)-central fatigue theory is provided and an explanation of how oral administration of BCAAs can decrease fatigue on the basis of this theory is given. The rate-limiting step in the synthesis of 5-HT is the transport of Trp across the blood-brain barrier. This transport is influenced by the fraction of Trp available for transport into the brain and the concentration of the other large neutral amino acids, including the BCAAs, which are transported via the same carrier system. During endurance exercise, there is an uptake of Trp by the brain, suggesting that this may increase the synthesis and release of 5-HT in the brain. Oral intake of BCAAs may reduce this uptake and also brain 5-HT synthesis and release, thereby delaying fatigue. Other hypotheses for the effect of BCAAs on central fatigue are included.
PMID: 16365097 [PubMed - indexed for MEDLINE]
A role for branched-chain amino acids in reducing central fatigue.
Blomstrand E.
Astrand Laboratory, University College of Physical Education and Sports and Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden. [email protected]
Several factors have been identified to cause peripheral fatigue during exercise, whereas the mechanisms behind central fatigue are less well known. Changes in the brain 5-hydroxytryptamine (5-HT) level is one factor that has been suggested to cause fatigue. The rate-limiting step in the synthesis of 5-HT is the transport of tryptophan across the blood-brain barrier. This transport is influenced by the fraction of tryptophan available for transport into the brain and the concentration of the other large neutral amino acids, including the BCAAs (leucine, isoleucine, and valine), which are transported via the same carrier system. Studies in human subjects have shown that the plasma ratio of free tryptophan (unbound to albumin)/BCAAs increases and that tryptophan is taken up by the brain during endurance exercise, suggesting that this may increase the synthesis of 5-HT in the brain. Ingestion of BCAAs increases their concentration in plasma. This may reduce the uptake of tryptophan by the brain and also 5-HT synthesis and thereby delay fatigue. Accordingly, when BCAAs were supplied to human subjects during a standardized cycle ergometer exercise their ratings of perceived exertion and mental fatigue were reduced, and, during a competitive 30-km cross-country race, their performance on different cognitive tests was improved after the race. In some situations the intake of BCAAs also improves physical performance. The results also suggest that ingestion of carbohydrates during exercise delays a possible effect of BCAAs on fatigue since the brain's uptake of tryptophan is reduced.
PMID: 16424144 [PubMed - indexed for MEDLINE]
Effect of infused branched-chain amino acids on muscle and whole-body amino acid metabolism in man.
Clin Sci (Lond). 1990 Nov;79(5):457-66.
Louard RJ, Barrett EJ, Gelfand RA.
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06510.
1. Using the forearm balance method, together with systemic infusions of L-[ring-2,6-3H]phenylalanine and L-[1-14C]leucine, we examined the effects of infused branched-chain amino acids on whole-body and skeletal muscle amino acid kinetics in 10 postabsorptive normal subjects; 10 control subjects received only saline. 2. Infusion of branched-chain amino acids caused a four-fold rise in arterial branched-chain amino acid levels and a two-fold rise in branched-chain keto acids; significant declines were observed in circulating levels of most other amino acids, including phenylalanine, which fell by 34%. Plasma insulin levels were unchanged from basal levels (8 +/- 1 mu-units/ml). 3. Whole-body phenylalanine flux, an index of proteolysis, was significantly suppressed by branched-chain amino acid infusion (P less than 0.002), and forearm phenylalanine production was also inhibited (P less than 0.03). With branched-chain amino acid infusion total leucine flux rose, with marked increments in both oxidative and non-oxidative leucine disposal (P less than 0.001). Proteolysis, as measured by endogenous leucine production, showed a modest 12% decrease, although this was not significant when compared with saline controls. The net forearm balance of leucine and other branched-chain amino acids changed from a basal net output to a marked net uptake (P less than 0.001) during branched-chain amino acid infusion, with significant stimulation of local leucine disposal. Despite the rise in whole-body non-oxidative leucine disposal, and in forearm leucine uptake and disposal, forearm phenylalanine disposal, an index of muscle protein synthesis, was not stimulated by infusion of branched-chain amino acids. 4. The results suggest that in normal man branched-chain amino acid infusion suppresses skeletal muscle proteolysis independently of any rise of plasma insulin. Muscle branched-chain amino acid uptake rose dramatically in the absence of any apparent increase in muscle protein synthesis, as measured by phenylalanine disposal, or in branched-chain keto acid release. Thus, an increase in muscle branched-chain amino acid concentrations and/or local branched-chain amino acid oxidation must account for the increased disposal of branched-chain amino acids.
PMID: 2174312 [PubMed - indexed for MEDLINE]
Leucine supplementation and intensive training.
Mero A.
Department of Biology of Physical Activity, University of Jyvaskyla, Finland. [email protected]
Leucine, isoleucine and valine, the branched-chain amino acids (BCAA), make up about one-third of muscle protein. Of these, leucine has been the most thoroughly investigated because its oxidation rate is higher than that of isoleucine or valine. Leucine also stimulates protein synthesis in muscle and is closely associated with the release of gluconeogenic precursors, such as alanine, from muscle. Significant decreases in plasma or serum levels of leucine occur following aerobic (11 to 33%), anaerobic lactic (5 to 8%) and strength exercise (30%) sessions. In skeletal muscle, there is a decrease in leucine level and a reduction in glycogen stores during exhaustive aerobic exercise. Basal fasting serum leucine levels decrease by 20% during 5 weeks of speed and strength training in power-trained athletes on a daily protein intake of 1.26 g/kg bodyweight. The leucine content of protein is assumed to vary between 5 and 10%. There are suggestions that the current recommended dietary intake of leucine be increased from 14 mg/kg bodyweight/day to a minimum of 45 mg/kg bodyweight/day for sedentary individuals, and more for those participating in intensive training in order to optimise rates of whole body protein synthesis. Consumption of BCAA (30 to 35% leucine) before or during endurance exercise may prevent or decrease the net rate of protein degradation, may improve both mental and physical performance and may have a sparing effect on muscle glycogen degradation and depletion of muscle glycogen stores. However, leucine supplementation (200 mg/kg bodyweight) 50 minutes before anaerobic running exercise had no effect on performance. During 5 weeks of strength and speed training, leucine supplementation of 50 mg/kg bodyweight/day, supplementary to a daily protein intake of 1.26 g/kg bodyweight/day, appeared to prevent the decrease in the serum leucine levels in power-trained athletes. According to 1 study, dietary supplementation of the leucine metabolite beta-hydroxy-beta-methylbutyrate (HMB) 3 g/day to humans undertaking intensive resistance training exercise resulted in an increased deposition of fat-free mass and an accompanying increase in strength. Muscle proteolysis was also decreased with HMB, accompanied by lower plasma levels of enzymes indicating muscle damage and an average 50% decrease in plasma essential amino acid levels. Furthermore, BCAA supplementation (76% leucine) in combination with moderate energy restriction has been shown to induce significant and preferential losses of visceral adipose tissue and to allow maintenance of a high level of performance. Caution must be paid when interpreting the limited number of studies in this area since, in many studies, leucine has been supplemented as part of a mixture of BCAA. Consequently, further research into the effects of leucine supplementation alone is needed.
PMID: 10418071 [PubMed - indexed for MEDLINE
From Poliquin (who loves to aminos):
4. The Miracle Of BCAA's
I strongly recommend that all of you use additional branched chain amino acid (BCAA) supplements (leucine, isoleucine, and valine), especially if your goal is to increase your lean body mass. I have learned several nutritional facts about the BCAA group from Eric Serrano, M.D., and Mauro Di Pasquale, M.D., and I have been using BCAAs with athletes who have difficulty gaining size.
It is not uncommon for individuals to gain 10 lbs. of muscle in 3-5 weeks of copious branched chain amino acid supplementation. Why does BCAA supplementation work so well? Consider:
Leucine is an important regulator of protein synthesis by reducing protein degradation in humans. Leucine spares glucose as fuel.
BCAAs promote protein synthesis.
BCAAs consumed during training raise growth hormone and insulin, hence the increased anti-catabolism and anabolism from BCAAs.
The BCAAs, unlike the other amino acids, can be used as a form of energy by muscle cells.
Carli et al. [1992] showed that supplementing with branched chain amino acids prior to a workout not only prevented a decrease in post-workout testosterone levels, but actually seemed to facilitate an increase in testosterone levels following exercise.
BCAA administration has a growth effect by enhancing the testosterone/cortisol ratio.
BCAA administration reduces exercise-induced increases in the muscle concentration of tyrosine and phenylalanine. This indicates that there is a decreased net rate of protein degradation during exercise.
Post workout soreness is reduced when you use BCAAs during training.
An Italian study on natural bodybuilders revealed that 0.2 g of BCAA per kg of bodyweight 30 minutes before workouts and 30 minutes after workouts led to greater increases in lean body mass, and strength gains in the bench press and squat.
BCAAs will decrease body fat (especially visceral fat, the fat that accumulates inside the abdomen and results in that beer gut look).
I recommend taking 0.44 gram of BCAAs per kilogram of bodyweight. If you weigh 90 kilograms (198 lbs.), that is about 40 grams of branched chain amino acids/day. If you are on a restricted budget, ingest 20 grams, or don't bother.
Over the years I have experimented with varying BCAA protocols - using them before, during and after workouts. My observations are that it is best to ingest them throughout the workout. This is as simple as taking 2-3 tablets between sets.
It was with this type of dosage, that we observed gains of up to 10 lbs. of lean body mass in just 3-4 weeks using this protocol!
"king of free stuff" / Retired
look for the raw bcaa powder which is much cheaper. Bulk nutrition springs to mind.
I use BCAAs pre and post cardio/workout when cutting.
AR-Hall of Famer
I find 10 grams works pretty well pre-workout; how much do you take pre- and post-workout?
"king of free stuff" / Retired
5g pre and post workout, same pre and post cardio and another 5g if i wake in the night for a pee!
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