Specifically using high quality protein such as whey protein contains an extraordinarily high amount of BCAA’s (over 30%). BCAA’s are known as the building blocks of muscle. BCAA’are made up of Leucine, Valine, and Isoleucine. Recently it has become known that taking 5 grams of Leucine with a protein shake or protein meal will increase protein synthesis by up to 70%. But the problem is that one can only buy L-Leucine, which is a single amino acid. This creates problems in the digestive tract as the body has trouble digesting single free form amino acids. Therefore, nutrition company’s and research groups that recommend using L-Leucine in hopes to increasing protein synthesis, instruct to take L-Leucine with food (other amino acids). But still this may not be enough for the body to digest and absorb the L-Leucine powder. To solve this problem, ProteinFactory.com is now offering Leucine Peptides. Leucine Peptides are in the form of di and tri peptides, or two or three amino acids linked together. The body absorbs amino acids through the intestinal tract and into the blood stream in the form of di and tri peptides. Our Leucine Peptides are made in the USA from the finest quality whey protein isolate and contains a complete amino acid profile including BCAA’s.
Serving size (1 tsp) 5 grams
Servings per pound: 90
If taken 3 times per day 1 pound will last 30 days.
Leucine peptides have an average MW of 16000 daltons
Instructions: Mix 1 tsp of Leucine Peptides with your protein shake or sprinkle on any protein meal. Do not exceed 4 times per day. Best time to use Leucine Peptides is post workout with a hydrolyzed protein like (PeptoPro, or Hydrolyzed 520) and a Carbohydrate. For beginners or those concerned with taste, use Leucine Peptides with one of our Whey Protein Isolates, like Native Whey Isolate or Ultra Amino 97 Whey Isolate
Leucine Regulates Translation Initiation of Protein Synthesis in Skeletal Muscle after Exercise
Layne E. Norton and Donald K. Layman
Division of Nutritional Sciences, Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, IL 61801
High-performance physical activity and post exercise recovery lead to significant changes in amino acid and protein metabolism in skeletal muscle. Central to these changes is an increase in the metabolism of the BCAA leucine. During exercise, muscle protein synthesis decreases together with a net increase in protein degradation and stimulation of BCAA oxidation. The decrease in protein synthesis is associated with inhibition of translation initiation factors 4E and 4G and ribosomal protein S6 under regulatory controls of intracellular insulin signaling and leucine concentrations. BCAA oxidation increases through activation of the branched-chain α-keto acid dehydrogenase (BCKDH). BCKDH activity increases with exercise, reducing plasma and intracellular leucine concentrations. After exercise, recovery of muscle protein synthesis requires dietary protein or BCAA to increase tissue levels of leucine in order to release the inhibition of the initiation factor 4 complex through activation of the protein kinase mammalian target of rapamycin (mTOR). Leucine’s effect on mTOR is synergistic with insulin via the phosphoinositol 3-kinase signaling pathway. Together, insulin and leucine allow skeletal muscle to coordinate protein synthesis with physiological state and dietary intake.