Review of Short Phrases and Links|
This Review contains major "Leucine"- related terms, short phrases and links grouped together in the form of Encyclopedia article.
- Leucine is the most common amino acid found in proteins, and is essential for optimal growth in infancy and childhood and for nitrogen equilibrium in adults.
- Leucine is a member of the branched-chain amino acid family, along with valine and isoleucine.
- Leucine is an essential amino acid and one of the branched-chain amino acids (the others are isoleucine and valine).
- Leucine is the most effective BCAA for preventing muscle loss because it breaks down and is converted to glucose more quickly than isoleucine and valine.
- Leucine is an essential amino acid, which cannot be manufactured in the body and is part of the three branched-chain-amino-acids.
- N-acyl ornithine was located in the cell membrane and N-acyl leucine and isoleucine in cytoplasm.
- The similarly sized amino acid isoleucine is 2.9 kcal mol-1 per residue less stabilizing than leucine, suggesting that leucine is well-packed.
- Synthetic amino acids include ornithine for lysine, fluorophenylalanine for phenylalanine, and norleucine for leucine or isoleucine.
- Leucine is completely ketogenic, valine is completely glucogenic, and isoleucine is both glucogenic and ketogenic.
- All amino acids except lysine and leucine are at least partly glucogenic.
- Not surprisingly, this results in a corresponding loss of leucine through catabolism (Boirie et al., 1997).
- An essential amino acid, C 6 H 13 NO 2, that is isomeric with leucine.
- Conversely, a negative leucine balance indicates conditions favoring protein catabolism.
- I n fact, whey actually produced a negative leucine balance.
- On the other hand, leucine absorption was increased in the tumor bearing groups.
- In contrast, leucine absorption was not increased in the N group.
- A positive leucine balance indicates a state (i.e., increased availability of leucine inside your muscle cells) that supports protein anabolism.
- Isoleucine is an isomer of leucine, and it contains two chiral carbon atoms.
- The interaction of methionine and leucine enkephalin with phosphatidylserine and phosphatidylcholine was studied by optical spectroscopy techniques.
- The structure of leucine was established by laboratory synthesis in 1891.
- Nutritional supplementation of the leucine metabolite beta-hydroxy-beta-methylbutyrate (hmb) during resistance training.
- The protein contains a leucine zipper motif and has high homology to predicted proteins from S. cerevisiae and C. elegans.
- Fig. 8. Rate of 1- 13 C-leucine incorporation into whole body proteins in young men receiving various intakes of dietary leucine.
- Alternative start codons (depending on the organism), include "GUG" or "UUG", which normally code for valine or leucine, respectively.
- Like isoleucine, leucine and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule.
- A nonpolar or hydrophobic R group can be a hydro-carbon chain, as in leucine.
- Specifically, each group of serine residues is either preceded or followed by a leucine residue.
- This leucine residue is universally conserved in GATA factors, and the conservative L683V change alters the binding affinity of the protein (17, 26).
- The upper case bold L represents a leucine residue from the genomic clone which corresponds to an isoleucine in P. carinii cd2 cDNA.
- In each instance, the alanyl-leucine dipeptide was found to exhibit less bitterness than free leucine.
- So we've covered the ketoisocaproic acid (KIC) component of Muscletech Leukic, let's take a quick look at the amino acid Leucine.
- Leucine Zipper: The leucine zipper domain is necessary for protein dimerization.
- The d position contains the conserved leucines found in the leucine zipper.
- We estimated a breakpoint for the relations between methionine intake and leucine oxidation and balance.
- The 24-h pattern and rate of leucine oxidation, with particular reference to tracer estimates of leucine requirements in healthy adults.
- Examples are leucine aminopeptidase, casepsin B, penicillin G acylase, and angiotensin converting enzyme.
- The element was used to determine leucine aminopeptidase in the following manner.
- Urine has also recently been tested to yieldinformation about leucine aminopeptidase.
- Body cell mass and leucine metabolism in cirrhosis.
- Thus, it has been suggested that HMB may partly be responsible for the benefits of leucine supplementation.
- They concluded that leucine supplementation during feeding improves muscle protein synthesis in the elderly subjects.
- Leucine helps in toning the body and the muscles.
- Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise.
- Leucine supplementation enhances skeletal muscle recovery in rats following exercise.
- Treatment The disorder is treated by a diet with moderate restriction of the amino acid leucine and supplementation of L-carnitine.
- On the other hand, in pregnant groups which received the leucine supplemented diet the absorption rate was 1.5 fold higher than non-pregnant group.
- A high amount of dietary leucine in the long-term depresses food intake and growth in various animals .
- Similarly, leucine and a complete meal were equally as effective at stimulating protein synthesis in fasted rats .
- Leucine works with the amino acids isoleucine and valine to repair muscles, regulate blood sugar, and provide the body with energy.
- Leucine also promotes the healing of bones, skin, and muscle tissue after traumatic injury, and is often recommended for those recovering from surgery.
- Eggs, pork, beef, chicken, pulses, soy beans, and leafy vegetables are good sources of leucine.
- Our range includes leucine, lysine, tryptophan and valine, their best sources are meat, fish, fowl, eggs and dairy products.
- The initial part of the pathway also leads to leucine.
- Leucine infusion appears to decrease protein degradation in humans (Nair et al., 1992).
- The very low levels in CFS patients of a by-product of protein degradation (leucine) that regulates this process suggests an ongoing proteolytic process.
- Four-hundred-fifty microliters of PRS were removed to measure the incorporation of [ 3 H]leucine into completed protein.
- People with depression, liver or kidney disease should avoid taking large amounts of leucine due to the changes of blood levels.
- OBJECTIVE: This study was designed to measure the effect of chronic alcohol intake on leucine turnover in outpatients with stable alcoholic liver cirrhosis.
- Basal rates of methionine and leucine turnover are summarized in Table 3 and Figure 2.
- Although it is clear that leucine is the most important of the BCAA's in stimulating protein synthesis, leucine supplementation alone is not recommended.
- While some data suggests that all three BCAAs are important for protein synthesis, leucine is the BCAA that has been the most well studied.
- These additional nutritional insights of leucine may have important applications in weight management and also in prevention and management of diabetes.
- HMB is a byproduct of leucine metabolism in the human body.
- Sequence analysis revealed that the third amino acid, a leucine in a majority of E peptides, was the most conserved (33).
- However, rates of leucine oxidation were much higher in the high protein group .
- For improved effect, administration of at least 3 grams of leucine per day, for example, may be preferred.
- In other words, a 5-gram dose should contain about 2.5 grams of leucine and 1.25 grams each of isoleucine and valine.
- I. General properties of the system and permeability of the cells for leucine and methionine.
- The equivalent residue to Asp-62 in Gal3p is Asp-56, and this was mutated to alanine and leucine.
- Biochemistry > Amino Acids > Essential Amino Acids > Valine
- Biochemistry > Amino Acids > Essential Amino Acids > Isoleucine
- Chemistry > Biochemistry > Amino Acids > Essential Amino Acids
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* Branched-Chain Amino Acids
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* Essential Amino Acids
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