Liquid amino acids vs capsules

[Built]

What is a sucker of sub vs intra?

 

[juggernaut]

What is a sucker of sub vs intra?

I was going to ask the same thing. Is there that much of a difference between using bcaas via injection?

 

[Author L. Rea]

2:1:1 ratio? Dude it's 4:1:1 these days!

Hello Captn: For rats that would be correct. Actual optimal Human physiology ratios depend upon rate of loss in GI shuttling, gluconeogenesis and ketonic responses as well as anabolism and building blocks for enzymes and lean tissue. If you are using less expensive standard free form hydrolyzed from whey/casein BCAAs the more Leucine the better as most is lost to various physiological processes such as mentioned prior. Therefore 8:1:1 would be more accurate though more a result of quality of the BCAAs not the BCAAs themselves. However, if high quality BCAAs created via the cane fermentation process and alpha-hydroxy technology are employed the human ratio changes to corrected amino acid pool and full body requirements which is 2.6:1.36:1.52 (Leucine:Isoleucine:Valine). Valine is higher in our pool/systemic exchange of BCAAs as a result of decreased Leucine utilization for oxidation due to increase liver Valine sacrifice for glutamine synthesis. Marketing and science do tend to conflict at times Bro.

Diabetes. 2006 Mar;55(3):675-81.
The greater contribution of gluconeogenesis to glucose production in obesity is related to increased whole-body protein catabolism.

Chevalier S, Burgess SC, Malloy CR, Gougeon R, Marliss EB, Morais JA.
Source

McGill Nutrition and Food Science Centre, McGill University Health Centre, Royal Victoria Hospital, 687 Pine Ave. West, Montreal, Quebec, Canada, H3A 1A1.

Abstract

Obesity is associated with an increase in the fractional contribution of gluconeogenesis (GNG) to glucose production. We tested if this was related to the altered protein metabolism in obesity. GNG(PEP) (via phosphoenol pyruvate [PEP]) was measured after a 17-h fast using the deuterated water method and 2H nuclear magnetic resonance spectroscopy of plasma glucose. Whole-body 13C-leucine and 3H-glucose kinetics were measured in the postabsorptive state and during a hyperinsulinemic-euglycemic-isoaminoacidemic clamp in 19 (10 men and 9 women) lean and 16 (7 men and 9 women) obese nondiabetic subjects. Endogenous glucose production was not different between groups. Postabsorptive %GNG(PEP) and GNG(PEP) flux were higher in obese subjects, and glycogenolysis contributed less to glucose production than in lean subjects. GNG(PEP) flux correlated with all indexes of adiposity and with postabsorptive leucine rate of appearance (Ra) (protein catabolism). GNG(PEP) was negatively related to the clamp glucose rate of disposal (Rd) and to the protein anabolic response to hyperinsulinemia. In conclusion, the increased contribution of GNG to glucose production in obesity is linked to increased postabsorptive protein catabolism and insulin resistance of both glucose and protein metabolism. Due to increased protein turnover rates, greater supply of gluconeogenic amino acids to the liver may trigger their preferential use over glycogen for glucose production.

Department of Food Science and Human Nutrition and yDivision of Nutritional Sciences, University of Illinois, Urbana, IL 16801

The BCAA leucine plays multiple roles in metabolism
beyond the minimum requirement as an essential substrate for
synthesis of new proteins (8,10). These roles include a key
regulator of translation initiation of protein synthesis in skeletal
muscle (11), a modulator of insulin/PI3-kinase signaling (12,13),
a fuel for skeletal muscle (14), and a primary nitrogen donor for
production of alanine and glutamine in skeletal muscle (15).
The potential for leucine to impact protein synthesis, insulin
signaling, and production of alanine and glutamine is dependent
on dietary intake and increasing leucine concentration in
skeletal muscle (8,10,13).
The multiple roles of leucine are, at least in part, associated
with absence of the branched-chain aminotransferase enzyme
in liver, resulting in an enriched supply of the BCAA appearing
in blood (8,10,16). Dietary BCAAs reach the blood virtually
unaltered from levels in the diet, allowing leucine to reach
skeletal muscle in direct proportion to dietary intakes. This is
a striking metabolic difference for these amino acids, which
account for .20% of total dietary protein. Using the traditional
thinking that dietary protein requirements should be defined by
efficiency of nitrogen handling, we are left to ponder why the
body evolved to metabolize 20% of total amino acids (and total
nitrogen) in peripheral tissues? We hypothesized that this
unique treatment of the BCAA and specifically leucine provides
an important signal of dietary quality for skeletal muscle
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