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EAA's vs. BCAA's

FishOrCutBait

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So I was gonna post a stupid question, but instead, I typed it into google.

(go figure) so now Im going to post the answer to my question for everyone else to read, and Ill summarize it.

From what I understand, in essence:

EAA's are best for bulking phases
BCAA's are best for cutting phases.

rdy set go

(Also, I didnt write this.)

Taken from View topic - Plates Chronicals.........Bcaa's vs. Eaa's. When & why. : Bodybuilding Forums and Fitness Forums by Prosource.net


"-BCAAs do not increase protein synthesis above basal levels, but they do decrease protein breakdown. They are very benificial while cutting and even may increase fat loss then. BCAAs seem to be the perfect supplement to use for people as a "midnight shake". It only gives you a few kcals. (20 kcal. since 5g will probably suffice) so you don't need to be afraid to gain fat mass compared to a midnight protein shake.

-**EAAs do increase protein synthesis above basal levels. This is what you want to use pre/post workout to increase muscle growth.

WHY BCAA'S FOR RECOVERY:
A) bcaas prevent protein breakdown, but do not increase protein synthesis.
B) Helps in fat loss while cutting.
C) Prevents a decrease in glutamine
D) Prevents muscle damage.

1)It is known that BCAA oxidation is promoted by exercise
2)Promotion of fatty acid oxidation upregulates the BCAA catabolism
3) 77 mg BCAAs/kg supplementation before exercise results in a large decrease in release of EAA, (531 +/- 70 mumol/kg) for BCAA vs. (924 +/- 148 mumol/kg) for control.
4) A cutting diet high in BCAAs increases body weight loss and % of fat loss more than a calorie restricted high protein cutting diet alone.
5)No toxic effects of BCAAs were observed at a dose of 2.5 g /kg for 3 mo or 1.25 g /kg for 1 y. There are no reports concerning BCAA toxicity in relation to exercise and sports at these levels.

***BCAAs prevent protein breakdown, but do not increase protein synthesis.

-Since 1978 a variety of studies have been performed in humans where BCAAs or leucine alone was administrated in varying amounts and durations. An anabolic effect of leucine and the branched-chain amino acids (BCAAs) on reduction of muscle protein breakdown was found in these studies, with no measured effect upon muscle protein synthesis. In addition, no untoward effects have been reported in any of these studies from infusion of the BCAAs at upward 3 times basal flux or 6 times normal dietary intake during the fed portion of the day.

-BCAA infusion in 10 post absorptive normal subjects causes a 4-fold rise in arterial BCAA levels. Plasma insulin levels were unchanged from basal levels. Whole-body phenylalanine flux, an index of proteolysis, was significantly suppressed by BCAA infusion. 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

-BCAAs during 1h cycle exercise and a 2h recovery period does not influence the rate of exchange of the aromatic AAs during exercise. In the recovery period, a faster decrease in the muscle concentration of aromatic AAs was found (46% compared with 25% in the placebo condition). There was also a tendency to a smaller release (an average of 32%) of these amino acids from the legs. The results suggest that BCAA have a protein-sparing effect during the recovery after exercise

-7.5-12 g BCAAs during intense exercise (a 30 km cross-country race and a full marathon) increases BCAA plasma and muscle concentration. In the placebo group plasma BCAA decreased and left muscle levels unchanged. The placebo group showed a 20-40% increase in the muscle concentration of aromatic AAs. BCAA supplementation prevented this increase in aromatic AAs in both muscle and plasma. These results suggest that an intake of BCAAs during exercise can prevent or decrease the net rate of protein degradation caused by heavy exercise

-77 mg BCAAs/kg supplementation before exercise resulted in a doubling (P < 0.05) of the arterial BCAA levels before exercise (339 +/- 15 vs. 822 +/- 86 microM). During the 60 min of exercise, the total release of BCAA was 68 +/- 93 vs. 816 +/- 198 mumol/kg (P < 0.05) for the BCAA and control trials, respectively. Furthermore, the increased intramuscular and arterial BCAA levels before and during exercise result in (???? thanks for finishing dude)

-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.

-In adipocytes from fed rats, the rate of fatty acid synthesis in the presence of glucose and insulin was inhibited 40% by valine (5 mm)

-Twenty-five competitive wrestlers restricted their caloric intake (28 kcal/kg per day) for 19 days. A high-BCAA diet provided 4 kg of weight loss, and 17.3% decrease in fat loss. There was no change in aerobic (VO2max) (p > 0.75) and anaerobic capacities (Wingate test) (p > 0.81), and in muscular strength (p > 0.82).

Prevents a decrease in glutamine
-Following an exercise bout, a decrease in plasma glutamine concentration can be observed, which is completely abolished by BCAA supplementation.

-BCAA supplementation during a triathlon completely prevents the decrease in plasma glutamine.......

Prevents muscle damage
-We hypothesized that BCAA supplementation would reduce the serum activities of intramuscular enzymes associated with muscle damage. 120 minutes exercise on a cycle ergometer significantly increases serum creatine kinase (CK) and lactate dehydrogenase (LDH) up to 5d post-exercise.....

-12 g BCAAs for 14d in 16 men (the exercise on day 7) significantly reduces this change in LDH and CK .

WHY ESSENTIAL AMINO ACIDS (EAAs) FOR RECOVERY:
A) EAAs increase protein synthesis above basal levels
B) Prevents muscle soreness

1) Nonessential amino acids are not necessary for stimulation of net muscle protein balance (6 g EAAs provides double the response of 3g EAA and 3g of nonessentail AA)
2) 40g EAAs does not increase net protein balance more than 20g EAAs
3) Ingestion of oral essential amino acids results in a change from net muscle protein degradation to net muscle protein synthesis after heavy resistance exercise in humans similar to that seen when the amino acids were infused.

EAAs increase protein synthesis above basal levels in depth.
-EAAs (essential amino acids) increases net muscle protein balance. 2x a day 6 g provides double the response of 2x a day 3 g.....

-Consumption of 40g EAAs after heavy resistance training results in a change from net protein degradation (-50 +/- 23 nmol. min) to net protein synthesis (29 +/- 14 nmol. min).......

-A 0.15g/kg/hr AA infusion for 3 hours in 6 normal men increases muscle protein synthesis by 141%. After exerecise this increase is 291%. Muscle protein breakdown was not significantly affected.....

-Consumption of 6g EAA + 35g sucrose immediately before exercise elevates response of net muscle protein synthesis more than consumption following exercise. Total net phenylalanine uptake across the leg was greater during PRE (209 /42 mg) than during POST (81/ 19mg).

-6g EAA'S consumed at 1 and 2 hours after resistance exercise increases protein synthesis (total net uptake of phenylalanine across the leg) (71 +/- 13 mg x leg x 3hr). Prior intake of amino acids and carbohydrate does not diminish the metabolic response to a second comparable dose ingested 1h later

Eaa's Prevent muscle soreness in depth.
-3.6 g AA's before and after exercise + 2 doses a day for 4 days after the exercise suppresses the rise in serum creatine kinase activity. This also diminished muscle soreness.

There is a lot of scientific data here!
To conclude..... take Bcaa's for dieting due to muscle sparing properties..... great during extended intense exercise and at bedtime....... take Eaa's before and after resistance training to increase protein synthesis...... I personally take Eaa's thru purple wraath supplementation.....controlled labs is a wonderful product but by all means they do not have a corner on the market and there are many great Amino Acid supplements out there.
Either way Amino acids should be a staple in any serious weight trained athelete, there is far too much scientific data to dismiss use of the all mighty Amino Acid...... Do yourself a favor if you do not have them in your supp. regimine, then you better add em because they are quite frankley just that important!

Peace,
Plates"
 
This is an old thread but being an avid user of BCAAs I find this very interesting. Especially ***BCAAs prevent protein breakdown, but do not increase protein synthesis

That sheds a whole new light on my fasted am training. Definitely going to look into EAA usage.
 
BCAAs definitely increase protein synthesis. In fact leucine alone has been shown to increase protein synthesis, via stimulation of the mtor pathway.

And 40g of EAAs is a bit ridiculous.

Also, it seems that some people actually prefer EAAs during a cut and use BCAAs during a bulk. In a caloric deficit you want all the essential aminos not just BCAAs. But during a bulk you can use BCAAs because you will be getting the other amino acids from your diet/protein comsumption. I think this rationale makes a lot of sense.
 
BCAAs definitely increase protein synthesis. In fact leucine alone has been shown to increase protein synthesis, via stimulation of the mtor pathway.

And 40g of EAAs is a bit ridiculous.

Also, it seems that some people actually prefer EAAs during a cut and use BCAAs during a bulk. In a caloric deficit you want all the essential aminos not just BCAAs. But during a bulk you can use BCAAs because you will be getting the other amino acids from your diet/protein comsumption. I think this rationale makes a lot of sense.

So you're saying the above post is incorrect that "BCAAs prevent protein breakdown, but do not increase protein synthesis"

Not being condesending, just asking. I train fasted first thing in the morning so protein breakdown and protein synthesis is very important to me...........and i find it interesting!!!

I'm not big on supps and actually found this on a search for "Purple Wraath" It's has been recommended to me for all it's goodies to supplement my up-coming low carb diet. Up until now i didn't look past straight BCAAs and Whey for my Amino Acid fix.
 
So you're saying the above post is incorrect that "BCAAs prevent protein breakdown, but do not increase protein synthesis"

Not being condesending, just asking. I train fasted first thing in the morning so protein breakdown and protein synthesis is very important to me...........and i find it interesting!!!

I'm not big on supps and actually found this on a search for "Purple Wraath" It's has been recommended to me for all it's goodies to supplement my up-coming low carb diet. Up until now i didn't look past straight BCAAs and Whey for my Amino Acid fix.

Yes, they are mistaken. Perform a google scholar search for bcaas and muscle protein synthesis and you will get many results showing it does increase it. Here's just one study that explains the situation quite well.

Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise.Blomstrand E, Eliasson J, Karlsson HK, Köhnke R.
Department of Surgical Science, Karolinska Institutet, Stockholm, Sweden. eva.blomstrand@gih.se

BCAAs (leucine, isoleucine, and valine), particularly leucine, have anabolic effects on protein metabolism by increasing the rate of protein synthesis and decreasing the rate of protein degradation in resting human muscle. Also, during recovery from endurance exercise, BCAAs were found to have anabolic effects in human muscle. These effects are likely to be mediated through changes in signaling pathways controlling protein synthesis. This involves phosphorylation of the mammalian target of rapamycin (mTOR) and sequential activation of 70-kD S6 protein kinase (p70 S6 kinase) and the eukaryotic initiation factor 4E-binding protein 1. Activation of p70 S6 kinase, and subsequent phopsphorylation of the ribosomal protein S6, is associated with enhanced translation of specific mRNAs. When BCAAs were supplied to subjects during and after one session of quadriceps muscle resistance exercise, an increase in mTOR, p70 S6 kinase, and S6 phosphorylation was found in the recovery period after the exercise with no effect of BCAAs on Akt or glycogen synthase kinase 3 (GSK-3) phosphorylation. Exercise without BCAA intake led to a partial phosphorylation of p70 S6 kinase without activating the enzyme, a decrease in Akt phosphorylation, and no change in GSK-3. It has previously been shown that leucine infusion increases p70 S6 kinase phosphorylation in an Akt-independent manner in resting subjects; however, a relation between mTOR and p70 S6 kinase has not been reported previously. The results suggest that BCAAs activate mTOR and p70 S6 kinase in human muscle in the recovery period after exercise and that GSK-3 is not involved in the anabolic action of BCAAs on human muscle.
 
I'm not sure why you'd want to supplement with EAA's - those are the same aminos that you get in abundance from eating lots of protein-packed foods. It seems like a waste of money for anyone whose diet can at least afford them enough calories to get in plenty of protein. As for BCAA's, they can be useful when dieting to prevent muscle loss, but they are very expensive. Not something you should be focusing your supp. money on if you are on a tight budget.
 
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