L-Glutamic Acid Hcl
L-Glutamine
L-Histidine
L-Histidine Hcl
L-Hydroxyproline
L-Isoleucine
L-Leucine
L-Lysine Acetate
L-Lysine Hcl
L-Methionine
L-Ornithine Hcl
L-Phenylalanine
L-Phenylglycine
L-Proline
L-Pyroglutamic Acid
L-Serine
L-Theanine
L-Threonine
L-Tryptophan
L-Tyrosine
L-Valine
L-Homoarginine Hcl
L-Citrulline
L-Homphenylalanine
L-Homoserine
L-Homocitrulline
DL-Alanine
DL-allo-Threonine
DL-Arginine HCL
DL-Aspartic Acid
DL-Carnitine HCL
DL-Cysteine
DL-Cystine
DL-Glutamic Acid
DL-Isoleucine
DL-Lysine Hcl
DL-Methionine
DL-Phenylalanine
DL-Phenylglycine
DL-Pyroglutamic Acid
DL-Serine
DL-Threonine
DL-Tryptophan
DL-Tyrosine
DL-Valine
DL-allo-Isoleucine
DL-Homocystine
DL-Homocysteine
DL-Homoserine
DL-Norvaline
D-Alanine
D-Arginine
D-Cycloserine
D-Cysteine
D-Glucosamine Hcl
D-Glutamic Acid
D-Glutamine
D-Histidine
D-Leucine
D-Methionine
D-Phenylglycine
D-Phenylalanine
D-Proline
D-Pyroglutamic Acid
D-Serine
D-Threonine
D-Tyrosine
D-Tryptophan
D-Valine
D-Asparagine
D-Aspartic Acid
D-Arginine Hcl
D-Histidine Hcl
D-Isoleucine
D-Norvaline
D-Ornitine Hcl

L-Alanine

(CAS: 56-41-7)

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Synonyms: L-¦Á-aminopropionic acid, (S)-2-aminopropionic acid

Molecular Formula: C3H7NO2
Molecular Weight: 89.09
CAS: 56-41-7
pKa (25 ˇăC): 2.35 (-COOH), 9.87 (-NH2) 1
Beilstein Registry No.: 1720248
EG/EC No.: 2002738
Specific rotation: +13.7ˇă to +15.1ˇă
(100 mg/ml, 6 M HCl, 25 ˇăC); +2.42ˇă
(100 mg/ml, H2O)2

Specification:
Assay: 98.5%-101.0%
Specific Rotation (after drying): +13.2ˇăˇ«+15.2ˇă
Lead: 10ppm Max
Heavy Metal: 0.002% Max
Loss on Drying: 0.3% Max
Residue of Ignition: 0.2% Max

L-Alanine was one of the first amino acids to be synthesized before its isolation from natural sources.In 1850, Strecker prepared alanine via the cyanohydrin reaction by reacting acetaldehyde and ammonia with hydrocyanic acid, and subsequent hydrolysis by HCl. The name alanine derives from the term aldehyde, reflecting one of the starting reagents.The isolation of alanine from natural sources was described by Sch¨ątzenberger and colleagues in 1875 and 1879 from silk and ovalbumin, respectively, and by Weyl in 1888 from silk fibroin. In amino acid metabolism, alanine reacts with ¦Á-ketoglutarate to yield pyruvate and glutamate.4 Alanine has been used as an amino donor in a study of the conversion of ketomethiobutyrate to methionine in several species of Bacillus. A study in Escherichia coli has utilized L-alanine to investigate protein expression related to adhesive factors. L-Alanine has been shown to enhance the rates of germination of Bacillus subtilis spores. L-Alanine is used in cell culture media and is a component of MEM nonessential amino acids solution.

L-Alanine can be used as food additive, health care cosmetics and so on.L(+)-alanine is a important raw material of VB6 production.

Preparation Instructions:This product is soluble in water (50 mg/ml), with heat as needed, yielding a clear, colorless solution.

L-Alanine is a non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system. BCAAs are used as a source of energy for muscle cells. During prolonged exercise, BCAAs are released from skeletal muscles and their carbon backbones are used as fuel, while their nitrogen portion is used to form another amino acid, Alanine. Alanine is then converted to Glucose by the liver. This form of energy production is called the Alanine-Glucose cycle, and it plays a major role in maintaining the body's blood sugar balance.

1. What is it and where does it come from?

L-alanine is a non-essential amino acid. It is an organic amino acid due to the presence of a carbon atom in its makeup. Alanine is found primarily in poultry, beef, pork and fish. Almost all animal based protein sources are rich in alanine. The contraction of muscle results in increased alanine levels within the body.

2. What does it do and what scientific studies give evidence to support this?

As an amino acid, alanine is used by the body as a building block of protein. Alanine plays a major role in transferring nitrogen from tissue sites in the body, to the liver. Alanine is also used by the body to draw upon blood sugar as an energy source.1

3. Who needs it and what are some symptoms of deficiency?

Everyone. Because alanine is used by the body to draw upon blood sugar as an energy source, it may prove useful for bodybuilders and other athletes who are attempting to reduce body fat levels. For the same reason, individuals who are obese or overweight may benefit by using a supplement containing alanine. When used in conjunction with arginine and glycine it has been demonstrated that an overall reduction in arterial plaque may result.

Diabetics, or individuals suffering from insulin insensitivity, may benefit from supplementing with alanine. Alanine has been shown to be important for the regulation of insulin.2 Alanine is also known to contribute to prostate health. For this reason, elderly males may benefit from its use.

4. How much should be taken? Are there any side effects?

No side effects have been reported, although as with any amino-acid, overdose is a possibility. Individuals suffering from diabetes, prostatitis or hypertension should consult a qualified medical practitioner prior to the use of supplemental L-alanine. Follow the directions as prescribed on the products label.

5. Where can I get it?

There are many different brand names that manufacture supplemental l-alanine. Below is a listing of all available brands that may be purchased here on Bodybuilding.com.

References:
1. Molecular Biology LabFax, Brown, T. A., ed., BIOS Scientific Publishers Ltd. (Oxford, UK: 1991), p. 29.
2. The Merck Index, 12th ed., Entry# 205.
3. The Chemistry of the Amino Acids, Volume 3,Greenstein, J. P., and Winitz, M., Robert E. Krieger Publishing Company (Malabar, FL: 1984), pp. 1819-1840.
4. Biochemistry, 3rd ed., Stryer, L., W. H. Freeman (New York, NY: 1988), pp. 504.
5. Berger, B. J., et al., Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J. Bacteriol., 185(8), 2418-2431 (2003).
6. Crost, C., et al., Leucine-responsive regulatory protein-mediated repression of clp (encoding CS31A) expression by L-leucine and L-alanine in Escherichia coli. J. Bacteriol., 185(6), 1886-1894 (2003).
7. Cabrera-Martinez, R. M., et al., Effects of overexpression of nutrient receptors on germination of spores of Bacillus subtilis. J. Bacteriol., 185(8), 2457-2464 (2003).