DL-TRYPTOPHAN

PRODUCT IDENTIFICATION

CAS NO. 54-12-6

DL-TRYPTOPHAN

EINECS NO.

200-194-9

FORMULA C11H12N2O2
MOL WT. 204.23

H.S. CODE

2933.99.1200

TOXICITY

Oral rat LD50: > 15000 mg/kg 
SYNONYMS H-DL-Trp-OH DL-Trytophane Racemic Tryptophan; (+-)-Tryptophan;
DL-alpha-Amino-3-indolepropionic acid;
SMILES c12c(C[C@@H](C(O)=O)N)c[nH]c1cccc2

CLASSIFICATION

Amino acid, Antidepressive, Psychotropic

EXTRA NOTES

Amino acid precursor of serotonin and melatonin

PHYSICAL AND CHEMICAL PROPERTIES

PHYSICAL STATE

white crystals

MELTING POINT Decomposes (289 C)
BOILING POINT  
SPECIFIC GRAVITY

 

SOLUBILITY IN WATER soluble
pH 5.5 - 7.0
VAPOR DENSITY

 

NFPA RATINGS

Health: 1 Flammability: 0 Reactivity: 0

REFRACTIVE INDEX

 

FLASH POINT

 

STABILITY

Stable under ordinary conditions. Moisture, light sensitive.

EXTERNAL LINKS & GENERAL DESCRIPTION

Wikipedia Linking

Google Scholar Search

Drug Information Portal (U.S. National Library of Medicine) - Tryptophan

PubChem Compound Summary - DL-Tryptophan

Drug Bank -  Tryptophan

KEGG (Kyoto Encyclopedia of Genes and Genomes) -  Tryptophan

http://www.ebi.ac.uk/chebi/ -  Tryptophan

http://www.ncbi.nlm.nih.gov/ -  Tryptophan

Human Metabolome Database - Tryptophan

Material Safety Data Sheet

http://www.iscid.org/
Tryptophan is an amino acid; one of the 20 found in the basic genetic code: codon UGG. It is essential in human nutrition, and may have significant effects on the human brain. Tryptophan is a precursor for serotonin, melatonin, and niacin. In those who cannot metabolize it properly, it's possible that tryptophan is a cause of schizophrenia. Improperly metabolized, its waste products are toxic to the brain and cause hallucinations and delusions. However, it's also been found to aid schizophrenic patients. Tryptophan is produced by the human body, but can also be found in many sources of dietary protein, including chocolate, oats, bananas, dried dates, cottage cheese, red meat, fish, milk, peanuts, and most famously turkey. According to a widespread myth, when the tryptophan in turkey is consumed, it is supposed to make the person consuming it very sleepy within a matter of hours. Whether this is fact or not is doubtful, especially the uniqueness of turkey. Still, tryptophan supplements have been used as a safe and somewhat effective sleep aid. This effect is probably because of its ability to increase brain levels of serotonin and melatonin. Serotonin is known for its calming effects, and melatonin, secreted by the pineal gland when dark or low light levels predominate, induces slumber. According to clinical research, tryptophan does act reasonably well as a sleep inducer, an antidepressant, and an augmentor of antidepressants. Chronic pain and reduction of negative extreme behaviors (impulsivity, mania, addiction, etc.) has also been indicated by researchers. And it may be effective in treating seasonal-affective disorder, or SAD. However, due to an outbreak of eosinophilia-myalgia syndrome (a sometimes-deadly autoimmune disease) traced to taking tryptophan from Japan, tryptophan supplements were banned by numerous companies. The problem was ultimately identified as probably a contaminant and not tryptophan at all, but the health agencies of many countries still remain leery of tryptophan. Despite this, psychiatrists continue to prescribe tryptophan as an antidepressant by itself or, more often, as an augmentor for other antidepressants in patients who are unresponsive to antidepressants.

Local:
Amino Acid is any of the organic compounds in which one (or more ) amino group (-NH2) and one (or more ) carboxylic acid group (-COOH) are both present with general formula R-CH(NH2)COOH containing carbon, hydrogen, oxygen, nitrogen, and in certain cases sulfur atoms. Two groups attached to the same carbon (called the alpha-carbon atom at the end of the compound) are polymerized to form peptides and proteins. The amine group is protonated to form -NH3+ at low pH. The carboxylic acid group is deprotonated to form -CO2- at high pH. The carbon atom in the carboxyl group of one amino acid binds covalently to the nitrogen atom in the amino group of another amino acid to form a peptide bond with the release of a water molecule. Proteins are synthesized through the covalent chemical polypeptide bonds. The sequence of these amino acids in the protein polypeptides determines the shape, properties, and hence biological role of the protein that function as chemical messengers and as intermediates in metabolism. Proteins are composed of various proportions of about 20 commonly occurring amino acids. Plants or other biological systems can synthesize amino acids from simple inorganic compounds, but animals rely on adequate supplies in their diet. More than 100 common amino acids occur in plants or in other microorganic systems. The 20 amino acids commonly found in animals are Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic Acid, Glutamine, Glycine, Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Proline, Serine, Threonine, Tryptophan, Tyrosine, and Valine. Many of the amino acids can be synthesized in the human or animal body from other cellular metabolites when needed (called Non-essential Amino Acids). Animals are not able to synthesize some amino acids necessary in metabolism in sufficient quantities. It must therefore be present in the diet (called Essential Amino Acids). In man, these essential amino acids are Arginine, Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan and Valine. Tryptophan is formed from proteins during digestion by the action of proteolytic enzymes and is necessary for normal growth and development. Branched amino-acids (Valine, Isoleucine and Leucine ) with tryptophan and phenylalanine (aromatic side chain amino acids) contribute to the structure of protein by the tendency of its side chain composed only of carbon and hydrogen to participate in hydrophobic interactions which determines the tertiary structure of the peptide chain. Infants require greater amounts of tryptophan than adults. Only the l-stereoisomer is biologically active form in mammalian protein. Tryptophan is also a precursor for serotonin (a neurotransmitter), melatonin (a neurohormone) and niacin (a vitamin of the B complex).

SALES SPECIFICATION

APPEARANCE

white crystals

ASSAY

98.0 - 101.0%

LOSS ON DRYING

0.3% max

RESIDUE ON IGNITION

0.1% max

NH4

0.02% max

CHLORIDE

0.02% max

SULFATE

0.02% max

HEAVY METALS

10ppm max

ARSENIC

1ppm max

TRANSPORTATION
PACKING
 
HAZARD CLASS Not regulated
UN NO.  
SAFETY INFORMATION
Hazard Symbols: n/a, Risk Phrases: 36/37/38, Safety Phrases: 24/25

GENERAL PROPERTIES OF AMINO ACIDS

Amino Acid

Abbreviation

Formula (Mol WT)

pK1

pK2

pKR

pI

Hydropathy Index

3-Letters

1-Letter

-COOH

-NH3+

R group

Alanine

Ala

A

C3H7NO2 (89.09)

2.34

9.69

-

6.00

1.8

Arginine

Arg

R

C6H14N4O2(174.20)

2.17

9.04

12.48

10.76

-4.5

Asparagine

Asn

N

C4H8N2O3(132.12)

2.02

8.80

-

5.41

-3.5

Aspartic Acid

Asp

D

C4H7NO4(133.10)

1.88

9.60

3.65

2.77

-3.5

Cysteine

Cys

C

C3H7NO2S(240.30)

1.96

10.128

8.18

5.07

2.5

Glutamic Acid

Glu

E

C5H9NO4(147.13)

2.19

9.67

4.25

3.22

-3.5

Glutamine

Gln

Q

C5H10N2O3(146.15)

2.17

9.13

-

5.65

-3.5

Glycine

Gly

G

C2H5O2(75.07)

2.34

9.60

-

5.97

-0.4

Histidine

His

H

C6H9N3O2(155.16)

1.82

9.17

6.00

7.59

-3.2

Isoleucine

Ile

I

C6H13NO2(131.18)

2.36

9.60

-

6.02

4.5

Leucine

Leu

L

C6H13NO2(131.18)

2.36

9.60

-

5.98

3.8

Lysine

Lys

K

C6H14N2O2(146.19)

2.18

8.95

10.53

9.74

-3.9

Methionine

Met

M

C5H11NO2S(149.21)

2.28

9.21

-

5.74

1.9

Phenylalanine

Phe

F

C9H11NO2(165.19)

1.83

9.13

-

5.48

2.8

Proline

Pro

P

C5H9NO2(115.13)

1.99

10.60

-

6.30

1.6

Serine

Ser

S

C3H7NO3(105.19)

2.21

9.15

-

5.58

-0.8

Threonine

Thr

T

C4H9NO3(119.12)

2.09

9.10

-

5.60

-0.7

Tryptophan

Trp

W

C11H10N2O2(204.23)

2.83

9.39

-

5.89

-0.9

Tyrosine

Tyr

Y

C9H11NO3(181.19)

2.20

9.11

10.07

5.66

-1.3

Valine

Val

V

C5H11NO2(117.15)

2.32

9.62

-

5.96

4.2

PRICE INFORMATION