L-Tryptophan

204.22500

204.23

200-795-6

8DUH1N11BX

757373

DTXSID5021419

C29603

Leaflets or plates from dilute alcohol|White to slightly yellowish-white ... crystals or crystalline powder

N - Nervous system

2933990090

79.11000

-1.1

L-tryptophan is a white powder with a flat taste. An essential amino acid; occurs in isomeric forms. (NTP, 1992)

1.4±0.1 g/cm3

282 °C

447.9°C at 760 mmHg

224.7±25.9 °C

1.698

H2O: 13.4 mg/mL at 25 °C

Protect from light

2.1X10-9 mm Hg at 25 deg C (est)

LD508mmol / kg (rat, intraperitoneal injection). It is safe when used in food (FDA, §172.320, 2000).

Specific optical rotation: -31.5 deg at 23 °C/D (water, 1%), +2.4 deg at 20 °C/D (hydrochloric acid, 0.5 N); +0.15 deg at 20 °C/D (sodium hydroxide, 2.43% in 0.5 N)

Odorless

FLAT TASTE

A 1% solution in water has a pH of 5.5 to 7.

7.38(at 25 °C)

7.38 (at 25 °C)|pK1 = 2.38 /SRC: carboxylic acid/; pK2 = 9.39 /SRC: primary amine/

154.22 Ų [M+H]+ [CCS Type: DT, Method: stepped-field]|158.58 Ų [M-H]- [CCS Type: DT, Method: stepped-field]|145 Ų [M+H]+ [CCS Type: TW, Method: calibrated with polyalanine]|150.1 Ų [M+H]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|150.3 Ų [M+H]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|147.6 Ų [M+Na]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|147.7 Ų [M+Na]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|142.3 Ų [M-H]- [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|142.5 Ų [M-H]- [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|151.5 Ų [M-H]- [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|149.1 Ų [M-H]-

Decomposes at 289 °C (rapid heating)|Needles from methanol, decomposes at 251 °C /Tryptophan hydrochloride/|UV: 3453 (Sadtler Research Laboratories Spectral Collection) /Tryptophan (DL)/

Slightly soluble in water.

Salts, Acidic

Acidic salts, such as L-TRYPTOPHAN, are generally soluble in water. The resulting solutions contain moderate concentrations of hydrogen ions and have pH's of less than 7.0. They react as acids to neutralize bases. These neutralizations generate heat, but less or far less than is generated by neutralization of inorganic acids, inorganic oxoacids, and carboxylic acid. They usually do not react as either oxidizing agents or reducing agents but such behavior is not impossible. Many of these compounds catalyze organic reactions.

NONH for all modes of transport

2

R33; R40; R62; R41; R37/38; R36/37/38; R22

S24/25; S36/37/39; S36; S26

YN6130000

F

Stable. Incompatible with strong acids, strong oxidizing agents.

P261, P264, P271, P280, P302+P352, P304+P340, P305+P351+P338, P312, P321, P332+P313, P337+P313, P362, P403+P233, P405, P501

H315

SRP: Criteria for land treatment or burial (sanitary landfill) disposal practices are subject to significant revision. Prior to implementing land disposal of waste residue (including waste sludge), consult with environmental regulatory agencies for guidance on acceptable disposal practices.|SRP: At the time of review, regulatory criteria for small quantity disposal are subject to significant revision, however, household quantities of waste pharmaceuticals may be managed as follows: Mix with wet cat litter or coffee grounds, double bag in plastic, discard in trash.|SRP: Expired or waste pharmaceuticals shall carefully take into consideration applicable DEA, EPA, and FDA regulations. It is not appropriate to dispose by flushing the pharmaceutical down the toilet or discarding to trash. If possible return the pharmaceutical to the manufacturer for proper disposal being careful to properly label and securely package the material. Alternatively, the waste pharmaceutical shall be labeled, securely packaged and transported by a state licensed medical waste contractor to dispose by burial in a licensed hazardous or toxic waste landfill or incinerator.

L-Tryptophan is a food additive permitted for direct addition to food for human consumption, as long as 1) the quantity of the substance added to food does not exceed the amount reasonably required to accomplish its intended physical, nutritive, or other technical effect in food, and 2) any substance intended for use in or on food is of appropriate food grade and is prepared and handled as a food ingredient.|Drug products containing certain active ingredients offered over-the-counter (OTC) for certain uses. A number of active ingredients have been present in OTC drug products for various uses, as described below. However, based on evidence currently available, there are inadequate data to establish general recognition of the safety and effectiveness of these ingredients for the specified uses: tryptophan is included in weight control drug products.

NAS, Food and Nutrition Board, Institute of Medicine; Dietary Reference Intakes for Energy, Carbohydrate, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids (Macronutrients). National Academy Press, Washington, D.C. (2009).[Available from, as of March 10, 2010: http://www.nap.edu/catalog/10490.html]|DHEW/NCI; Bioassay of L-Tryptophan for Possible Carcinogenicity CAS No. 73-22-3 (NCI-CG-TR-71) (1978) Technical Report Series No. 71 DHEW Pub No. (NIH) 78-1321[Available from, as of March 29, 2010: http://ntp.niehs.nih.gov/ntp/htdocs/LT_rpts/tr071.pdf]

Flash point data for this chemical are not available. It is probably combustible. (NTP, 1992)

Not Classified

Fires involving this material should be controlled using a dry chemical, carbon dioxide or Halon extinguisher. (NTP, 1992)

SMALL SPILLS AND LEAKAGE: If you spill this chemical, you should dampen the solid spill material with water, then transfer the dampened material to a suitable container. Use absorbent paper dampened with water to pick up any remaining material. Seal your contaminated clothing and the absorbent paper in a vapor-tight plastic bag for eventual disposal. Wash all contaminated surfaces with a soap and water solution. Do not reenter the contaminated area until the Safety Officer (or other responsible person) has verified that the area has been properly cleaned. STORAGE PRECAUTIONS: You should keep this material in a tightly-closed container under an inert atmosphere, and store it in a refrigerator. (NTP, 1992)

RECOMMENDED RESPIRATOR: Where the neat test chemical is weighed and diluted, wear a NIOSH-approved half face respirator equipped with an organic vapor/acid gas cartridge (specific for organic vapors, HCl, acid gas and SO2) with a dust/mist filter. (NTP, 1992)

Oral rat LD50: > 16 gm/kg. Investigated as a tumorigen, mutagen, reproductive effector. Symptoms of overdose include agitation, confusion, diarrhea, fever, overactive reflexes, poor coordination, restlessness, shivering, sweating, talking or acting with excitement you cannot control, trembling or shaking, twitching, and vomiting.

Acetylsalicylic acid reduced serum-protein binding of tryptophan in man, causing rise in free serum tryptophan. Changes in metabolic pattern also occurred, with increased urinary excretion of xanthurenic acid and 3-hydroxylkynurenine and decreased excretion of 3-hydroxyanthranilic acid.|Although tryptophan has been given to patients receiving MAOIs in the belief that clinical efficacy may be improved, it should be noted that the adverse effects may also be potentiated.|Use of tryptophan with drugs that inhibit the reuptake of serotonin may exacerbate the adverse effects of the latter and precipitate the serotonin syndrome.|There have been occasional reports of sexual disinhibition in patients taking tryptophan with phenothiazines or benzodiazepines.|For more Interactions (Complete) data for (L)-Tryptophan (16 total), please visit the HSDB record page.

LD50 Rat ip 1634 mg/kg|LD50 Mouse ip 4800 mg/kg

A bioassay of the amino acid L-tryptophan for possible carcinogenicity was conducted by administering the test compound to Fischer 344 rats and B6C3F1 mice. Groups of 35 rats and 35 mice of each sex were administered the test compound at one of two doses, either 25,000 or 50,000 ppm, 5 day/wk for 78 wk, and then observed for 26 or 27 wk. Matched controls consisted of groups of 15 rats or 15 mice of each sex. All surviving rats and mice were sacrificed at 104 or 105 wk ... No neoplasms occurred in a statistically significant incidence among dosed rats when compared with controls. In both male and female mice, neoplasms of the hematopoietic system occurred at higher incidences in the low dose groups than in the matched control groups ... These incidences, however, are not statistically significant, ... therefore, no tumors are considered to be related to the administration of the test chemical ... It is concluded that under the conditions of this bioassay, L-tryptophan was not carcinogenic for Fischer 344 rats or B6C3F1 mice.

(L)-Tryptophan is an essential amino acid for human development and a precursor of serotonin(1).|MILK & EGGS ... HAVE HIGH TRYPTOPHAN CONTENT.

(L)-Tryptophan's production and use in nutrition and research, in medicine, as a dietary supplement, and in cereal enrichment(1) may result in its release to the environment through various waste streams(SRC).

TERRESTRIAL FATE: Based on a classification scheme(1), an estimated Koc value of 320(SRC), determined from a log Kow of -1.06(2) and a regression-derived equation(3), indicates that (L)-tryptophan is expected to have moderate mobility in soil(SRC). The pKa values of pKa1 2.38 (carboxylic acid) and pKa2 9.39 (primary amine)(4) indicate that this compound will exist as a zwitterion which may affect its adsorption to soils and sediments(SRC). Volatilization from moist soil is not expected because ions do not volatilize(SRC). Volatilization from moist soil is not expected because the acid/base exists as an anion/cation and anions/cations do not volatilize. (L)-Tryptophan is not expected to volatilize from dry soil surfaces(SRC) based upon an estimated vapor pressure of 2.1X10-9 mm Hg at 25 °C(SRC), determined from a fragment constant method(5). Using the Warburg respirometer test, a theoretical BOD value of 4.6% in 24 hours(6) suggests that biodegradation is not expected to be an important environmental fate process in soil(SRC).|AQUATIC FATE: Based on a classification scheme(1), an estimated Koc value of 320(SRC), determined from a log Kow of -1.06(2) and a regression-derived equation(3), indicates that (L)-tryptophan may adsorb to suspended solids and sediment(SRC). The pKa values of pKa1 2.38 (carboxylic acid) and pKa2 9.39 (primary amine)(4) indicate (L)-tryptophan will exist as a zwitterion at pH values of 5 to 9 and therefore volatilization from water surfaces is not expected to be an important fate process(5). According to a classification scheme(6), an estimated BCF of 3(SRC), from its log Kow(2) and a regression-derived equation(7), suggests the potential for bioconcentration in aquatic organisms is low(SRC). Using the Warburg respirometer test, a theoretical BOD value of 4.6% in 24 hours(8) suggests that biodegradation is not expected to be an important environmental fate process in water(SRC).|ATMOSPHERIC FATE: According to a model of gas/particle partitioning of semivolatile organic compounds in the atmosphere(1), (L)-tryptophan, which has an estimated vapor pressure of 2.1X10-9 mm Hg at 25 °C(SRC), determined from a fragment constant method(2), is expected to exist solely in the particulate phase in the ambient atmosphere. Particulate-phase (L)-tryptophan may be removed from the air by wet or dry deposition(SRC). Photooxidation proceeds primarily by a singlet-oxygen mechanism(3). The oxidation products kynurenine and N-formylkynurenine accumulated most readily at pH 4-7.5 following irradiation of solutions of tryptophan containing riboflavin(4).

(L)-Tryptophan is not expected to undergo hydrolysis in the environment due to the lack of functional groups that hydrolyze under environmental conditions(1). (L)-Tryptophan in aqueous solution was shown to photodegrade readily over six hours using both an HPLN-N 125 W Phillips lamp as a the near-UV source and natural sunlight(2). Photooxidation proceeds primarily by a singlet-oxygen mechanism(3). The oxidation products kynurenine and N-formylkynurenine accumulated most readily at pH 4-7.5 following irradiation of solutions of tryptophan containing riboflavin(4).

An estimated BCF of 3 was calculated in fish for (L)-tryptophan(SRC), using a log Kow of -1.06(1) and a regression-derived equation(2). According to a classification scheme(3), this BCF suggests the potential for bioconcentration in aquatic organisms is low(SRC).

The Koc of (L)-tryptophan is estimated as 320(SRC), using a log Kow of -1.06(1) and a regression-derived equation(2). According to a classification scheme(3), this estimated Koc value suggests that (L)-tryptophan is expected to have moderate mobility in soil. The pKa values of pKa1 2.38 (carboxylic acid) and pKa2 9.39 (primary amine)(4) indicate that this compound will exist as a zwitterion which may affect its adsorption to soils and sediments(SRC).

The pKa values of pKa1 2.38 (carboxylic acid) and pKa2 9.39 (primary amine)(1) indicate (L)-tryptophan will exist as a zwitterion at pH values of 5 to 9 and therefore volatilization from water surfaces is not expected to be an important fate process(2). (L)-Tryptophan is not expected to volatilize from dry soil surfaces(SRC) based upon an estimated vapor pressure of 2.1X10-9 mm Hg(SRC), determined from a fragment constant method(3).

Concentrations of tryptophan (free and protein bound) and its metabolites in ... breast milk were determined by high performance liquid chromatography. ... The colostrum contained a high level of total tryptophan. There were high ratios of free to total tryptophan in colostrum, transitional and mature milk. ...

NIOSH (NOES Survey 1981-1983) has statistically estimated that 24,809 workers (2,015 of these were female) were potentially exposed to (L)-tryptophan in the US(1). Occupational exposure to (L)-tryptophan may occur through inhalation and dermal contact with this compound at workplaces where (L)-tryptophan is produced or used. Use data indicate that the general population may be exposed to (L)-tryptophan via ingestion of food and other consumer products containing (L)-tryptophan(SRC).

Concentrations of tryptophan (free and protein bound) and its metabolites in plasma of maternal vein at delivery, umbilical vein, umbilical artery, neonatal vein and breast milk were determined by high performance liquid chromatography. The plasma levels of tryptophan and most of its metabolites in umbilical vein and artery were significantly higher than those in maternal vein. The concentration of total tryptophan in plasma of neonatal vein showed marked decrease at 24 h after birth in comparison with that at birth, but the total kynurenine concentration was not decreased in plasma of neonatal vein. The colostrum contained a high level of total tryptophan. There were high ratios of free to total tryptophan in colostrum, transitional and mature milk. In the blood, ratios of free to total of tryptophan and kynurenine were kept at constant level throughout the perinatal period.

Tryptophan may be useful in increasing serotonin production, promoting healthy sleep, managing depression by enhancing mental and emotional well-being, managing pain tolerance, and managing weight.|Parenteral nutrition|Supplementation of amino-acids where parenteral nutrition is required.

Tryptophan is a precursor of serotonin. Because CNS depletion of serotonin is considered to be involved in depression, tryptophan has been used in its treatment. Although it has been given alone, evidence of effectiveness is scant and tryptophan has generally been used as adjunctive therapy in depression. It has sometimes been given with pyridoxine and ascorbic acid, which are involved in its metabolism to serotonin|/EXPTL USE/: Inhibition of Walker 256 intramuscular carcinoma in rats by admin of l-tryptophan.|(L)-Tryptophan decreases sleep latency and slightly increases sleeping time without altering qualitative characteristics of polygraphic patterns during sleep in normal subjects. In insomniac patients, it increases sleeping time and decreases both sleep latency and number of awakenings.|Beneficial effects were observed when L-tryptophan was administered to 2 patients with myoclonus. In each case suspension of methylcellulose and water containing 1 g of (L)-tryptophan/15 mL was prepared and administered orally at a level of 10 g daily in 5 divided doses.|For more Therapeutic Uses (Complete) data for (L)-Tryptophan (11 total), please visit the HSDB record page.

Since serotonin plays a role in inducing and maintaining sleep, l-tryptophan has been administered orally to increase brain levels of serotonin. Although a dose of 1 g significantly decreased sleep latency and total time awake without altering sleep patterns, the hypnotic action is observed only during the early part of the sleep cycle, is unpredictable, and is not characterized by a satisfactory dose-response relationship. Because the hypnotic action has not been confirmed in other studies, this use of l-tryptophan must be considered investigational and the drug is not recommended in routine clinical practice. In order to avoid central serotonergic toxicity, tryptophan should not be used in patients also receiving a monoamine oxidase inhibitor or the serotonin uptake inhibitor, fluoxetine (Prozac).|Tryptophan-containing products have been associated with the eosinophilia-myalgia syndrome. Other adverse effects that have been reported include nausea, headache, lightheadedness, and drowsiness.|An increased incidence of bladder tumours has been reported in mice given l-tryptophan orally as well as in cholesterol pellets embedded in the bladder lumen. However, there was no increase in tumour incidence when only high-dose, oral tryptophan was given.|Tryptophan has been associated with eosinophilia-myalgia syndrome; caution is advised in patients receiving the drug who develop some, but not all, of the symptoms of this syndrome. It should not be used in those with a history of eosinophilia-myalgia syndrome associated with tryptophan treatment.|For more Drug Warnings (Complete) data for (L)-Tryptophan (7 total), please visit the HSDB record page.

Tryptophan is critical for the production of the body's proteins, enzymes and muscle tissue. It is also essential for the production of niacin, the synthesis of the neurotransmitter serotonin and melatonin. Tryptophan supplements can be used as natural relaxants to help relieve insomnia. Tryptophan can also reduce anxiety and depression and has been shown to reduce the intensity of migraine headaches. Other promising indications include the relief of chronic pain, reduction of impulsivity or mania and the treatment of obsessive or compulsive disorders. Tryptophan also appears to help the immune system and can reduce the risk of cardiac spasms. Tryptophan deficiencies may lead to coronary artery spasms. Tryptophan is used as an essential nutrient in infant formulas and intravenous feeding. Tryptophan is marketed as a prescription drug (Tryptan) for those who do not seem to respond well to conventional antidepressants. It may also be used to treat those afflicted with seasonal affective disorder (a winter-onset depression). Tryptopan serves as the precursor for the synthesis of serotonin (5-hydroxytryptamine, 5-HT) and melatonin (N-acetyl-5-methoxytryptamine).

A structurally and mechanistically diverse group of drugs that are not tricyclics or monoamine oxidase inhibitors. The most clinically important appear to act selectively on serotonergic systems, especially by inhibiting serotonin reuptake. (See all compounds classified as Antidepressive Agents, Second-Generation.)

(L)-Tryptophan with plant oils in soft gelatin capsules permitted lower dosage than with usual dosage form. Max of free tryptophan in serum was achieved in 1st hr whereas 4-5 times as much would be required with tablets or hard gelatin capsules.|Absorption and Fate. Tryptophan is readily absorbed from the gastro-intestinal tract. Tryptophan is extensively bound to serum albumin. It is metabolized to serotonin and other metabolites, incl kynurenine derivatives, and excreted in the urine. Pyridoxine and ascorbic acid appear to be concerned in its metabolism.|Although the free amino acids dissolved in the body fluids are only a very small proportion of the body's total mass of amino acids, they are very important for the nutritional and metabolic control of the body's proteins. ... Although the plasma compartment is most easily sampled, the concentration of most amino acids is higher in tissue intracellular pools. Typically, large neutral amino acids, such as leucine and phenylalanine, are essentially in equilibrium with the plasma. Others, notably glutamine, glutamic acid, and glycine, are 10- to 50-fold more concentrated in the intracellular pool. Dietary variations or pathological conditions can result in substantial changes in the concentrations of the individual free amino acids in both the plasma and tissue pools. /Amino acids/|After ingestion, proteins are denatured by the acid in the stomach, where they are also cleaved into smaller peptides by the enzyme pepsin, which is activated by the increase in stomach acidity that occurs on feeding. The proteins and peptides then pass into the small intestine, where the peptide bonds are hydrolyzed by a variety of enzymes. These bond-specific enzymes originate in the pancreas and include trypsin, chymotrypsins, elastase, and carboxypeptidases. The resultant mixture of free amino acids and small peptides is then transported into the mucosal cells by a number of carrier systems for specific amino acids and for di- and tri-peptides, each specific for a limited range of peptide substrates. After intracellular hydrolysis of the absorbed peptides, the free amino acids are then secreted into the portal blood by other specific carrier systems in the mucosal cell or are further metabolized within the cell itself. Absorbed amino acids pass into the liver, where a portion of the amino acids are taken up and used; the remainder pass through into the systemic circulation and are utilized by the peripheral tissues. /Amino acids/|For more Absorption, Distribution and Excretion (Complete) data for (L)-Tryptophan (9 total), please visit the HSDB record page.

Hepatic.|In Hartnup disease ... tryptophane appear/s/ in urine due to defective renal and intestinal absorption of tryptophane ... It is an intermediary metabolite in the synthesis of serotonin (5-hydroxytryptamine) and 5-hydroxyindole acetic acid (HIAA).|Patients with bladder cancer excreted significantly more kynurenic acid, acetylkynurenine, kynurenine, and 3-hydroxykynurenine after ingesting a loading dose of L-tryptophan than did control subjects with no known disease.|Tryptophan is metabolized in the liver by tryptophan pyrrolase and tryptophan hydroxylase. Metabolites include hydroxytryptophan, which is then converted to serotonin, and kynurenine derivatives. Some tryptophan is converted to nicotinic acid and nicotinamide. Pyridoxine and ascorbic acid are cofactors in the decarboxylation and hydroxylation, respectively, of tryptophan; pyridoxine apparently prevents the accumulation of the kynurenine metabolites.|Yields indole-3-pyruvic acid in man ... and in rats; yields tryptamine in guinea pigs. /From table/|For more Metabolism/Metabolites (Complete) data for (L)-Tryptophan (21 total), please visit the HSDB record page.

The biological half-life of tryptophan was reported to be 15.8 hr.

A number of important side reactions occur during the catabolism of tryptophan on the pathway to acetoacetate. The first enzyme of the catabolic pathway is an iron porphyrin oxygenase that opens the indole ring. The latter enzyme is highly inducible, its concentration rising almost 10-fold on a diet high in tryptophan. Kynurenine is the first key branch point intermediate in the pathway. Kynurenine undergoes deamniation in a standard transamination reaction yielding kynurenic acid. Kynurenic acid and metabolites have been shown to act as antiexcitotoxics and anticonvulsives. A second side branch reaction produces anthranilic acid plus alanine. Another equivalent of alanine is produced further along the main catabolic pathway, and it is the production of these alanine residues that allows tryptophan to be classified among the glucogenic and ketogenic amino acids. The second important branch point converts kynurenine into 2-amino-3-carboxymuconic semialdehyde, which has two fates. The main flow of carbon elements from this intermediate is to glutarate. An important side reaction in liver is a transamination and several rearrangements to produce limited amounts of nicotinic acid, which leads to production of a small amount of NAD⁺ and NADP⁺.|Findings indicate that enhanced rates of serotonin turnover produced by (L)-tryptophan and physical restraint are associated with inhibition of thyroid-stimulating hormone (TSH) and stimulation of prolactin release from anterior pituitary in rats.|L-Tryptophan, an indispensable amino acid, serves as a precursor for several small molecules of functional significance including the vitamin niacin, the neurotransmitter serotonin, the metabolite tryptamine, and the pineal hormone melatonin. Increases in tryptophan have been shown to increase synthesis of the neurotransmitters in brain, blood, and other body organs.|Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Amino acids/|The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome.|For more Mechanism of Action (Complete) data for (L)-Tryptophan (7 total), please visit the HSDB record page.

ACUTE/CHRONIC HAZARDS: When heated to decomposition this compound emits toxic fumes. (NTP, 1992)

EYES: First check the victim for contact lenses and remove if present. Flush victim's eyes with water or normal saline solution for 20 to 30 minutes while simultaneously calling a hospital or poison control center. Do not put any ointments, oils, or medication in the victim's eyes without specific instructions from a physician. IMMEDIATELY transport the victim after flushing eyes to a hospital even if no symptoms (such as redness or irritation) develop. SKIN: IMMEDIATELY flood affected skin with water while removing and isolating all contaminated clothing. Gently wash all affected skin areas thoroughly with soap and water. If symptoms such as redness or irritation develop, IMMEDIATELY call a physician and be prepared to transport the victim to a hospital for treatment. INHALATION: IMMEDIATELY leave the contaminated area; take deep breaths of fresh air. If symptoms (such as wheezing, coughing, shortness of breath, or burning in the mouth, throat, or chest) develop, call a physician and be prepared to transport the victim to a hospital. Provide proper respiratory protection to rescuers entering an unknown atmosphere. Whenever possible, Self-Contained Breathing Apparatus (SCBA) should be used; if not available, use a level of protection greater than or equal to that advised under Protective Clothing. INGESTION: DO NOT INDUCE VOMITING. If the victim is conscious and not convulsing, give 1 or 2 glasses of water to dilute the chemical and IMMEDIATELY call a hospital or poison control center. Be prepared to transport the victim to a hospital if advised by a physician. If the victim is convulsing or unconscious, do not give anything by mouth, ensure that the victim's airway is open and lay the victim on his/her side with the head lower than the body. DO NOT INDUCE VOMITING. IMMEDIATELY transport the victim to a hospital. (NTP, 1992)

/SRP:/ Immediate first aid: Ensure that adequate decontamination has been carried out. If patient is not breathing, start artificial respiration, preferably with a demand valve resuscitator, bag-valve-mask device, or pocket mask, as trained. Perform CPR if necessary. Immediately flush contaminated eyes with gently flowing water. Do not induce vomiting. If vomiting occurs, lean patient forward or place on the left side (head-down position, if possible) to maintain an open airway and prevent aspiration. Keep patient quiet and maintain normal body temperature. Obtain medical attention. /Poisons A and B/|/SRP:/ Basic treatment: Establish a patent airway (oropharyngeal or nasopharyngeal airway, if needed). Suction if necessary. Watch for signs of respiratory insufficiency and assist ventilations if needed. Administer oxygen by nonrebreather mask at 10 to 15 L/min. Monitor for pulmonary edema and treat if necessary ... . Monitor for shock and treat if necessary ... . Anticipate seizures and treat if necessary ... . For eye contamination, flush eyes immediately with water. Irrigate each eye continuously with 0.9% saline (NS) during transport ... . Do not use emetics. For ingestion, rinse mouth and administer 5 mL/kg up to 200 mL of water for dilution if the patient can swallow, has a strong gag reflex, and does not drool ... . Cover skin burns with dry sterile dressings after decontamination ... . /Poisons A and B/|/SRP:/ Advanced treatment: Consider orotracheal or nasotracheal intubation for airway control in the patient who is unconscious, has severe pulmonary edema, or is in severe respiratory distress. Positive-pressure ventilation techniques with a bag valve mask device may be beneficial. Consider drug therapy for pulmonary edema ... . Consider administering a beta agonist such as albuterol for severe bronchospasm ... . Monitor cardiac rhythm and treat arrhythmias as necessary ... . Start IV administration of D5W /SRP: "To keep open", minimal flow rate/. Use 0.9% saline (NS) or lactated Ringer's if signs of hypovolemia are present. For hypotension with signs of hypovolemia, administer fluid cautiously. Watch for signs of fluid overload ... . Treat seizures with diazepam or lorazepam ... . Use proparacaine hydrochloride to assist eye irrigation ... . /Poisons A and B/

/HUMAN EXPOSURE STUDIES/ Serotonin and its metabolite 5-hydroxyindoleacetic acid (5-HIAA) in human blood and brain cerebrospinal fluid (CSF) increase /were found/ after tryptophan loading, which is similar to the effects of L-tryptophan in animals. ... Elevations in blood and 5-HIAA and CSF serotonin after single doses of 3 or 6 g of L-tryptophan. However, ... a double-blind, placebo-controlled trial in six normal men fed 3 g/day of L-tryptophan in divided doses with meals for 3 days, found a 113% elevation in plasma tryptophan, but no changes in platelet or plasma serotonin or in plasma catecholamines. ... No changes in urinary catecholamines /were found/. Additionally, no changes in blood pressure, heart rate, plasma sodium levels or 24-hour sodium excretion in urine /were found/.|/HUMAN EXPOSURE STUDIES/ L-Tryptophan administration (2 g) as a single dose before a meal has been found to decrease subjective hunger ratings, food intake, and alertness in men, but not women.|/HUMAN EXPOSURE STUDIES/ 15 humans /were tested/ only once with 0, 1, 2, and 3 g of L-tryptophan. Individuals receiving 2 and 3 g of L-tryptophan had decreased hunger and alertness and increased faintness and dizziness. Administration of 1 g of L-tryptophan with 10 g of carbohydrates before each meal (3 g L-tryptophan/d) for 3 months did not affect body weight of obese humans.|/HUMAN EXPOSURE STUDIES/ Daily doses of 2.4 g of L-tryptophan for 2 weeks did not produce a significant reduction in the consumption of carbohydrate snacks in the majority of the 24 individuals.|For more Human Toxicity Excerpts (Complete) data for (L)-Tryptophan (19 total), please visit the HSDB record page.

Ardeydorm

Grades: Reagent; Technical; Food Chemicals Codex /Tryptophan/|(L)-Tryptophan with plant oils in soft gelatin capsules.

L-Tryptophan: ACTIVE|An essential amino acid for human development; precursor of serotonin.|60 mg of tryptophan is approx equiv to 1.0 mg of niacin. /Tryptophan/|The amino acids that are incorporated into mammalian protein are alpha-amino acids, with the exception of proline, which is an alpha-imino acid. This means that they have a carboxyl group, an amino nitrogen group, and a side chain attached to a central alpha-carbon. Functional differences among the amino acids lie in the structure of their side chains. In addition to differences in size, these side groups carry different charges at physiological pH (e.g., nonpolar, uncharged but polar, negatively charged, positively charged); some groups are hydrophobic (e.g., branched chain and aromatic amino acids) and some hydrophilic (most others). These side chains have an important bearing on the ways in which the higher orders of protein structure are stabilized and are intimate parts of many other aspects of protein function.

Method: AOAC 960.47; Procedure: microbiological, turbidimetric and titrimetric methods; Analyte: tryptophan; Matrix: vitamin preparations; Detection Limit: not provided.|Method: AOAC 988.15; Procedure: ion exchange chromatographic method; Analyte: tryptophan; Matrix: foods and food & feed ingredients; Detection Limit: not provided.|TECHNIQUE OF DOUBLE-BEAM FLUORESCENCE SPECTROPHOTOMETRY FOR DETERMINATION OF TRYPTOPHAN IN PROTEINS.|Determination of tryptophan in foods by isocratic reversed-phase HPLC.

The plasma levels of 5-HT and its metabolites were determined by a HPLC system coupled with an amperometric detector. The HPLC system uses a reversed-phase column IRICA RP-18, with 4-hydroxyphenylacetic acid as internal std. The detection sensitivity of the HPLC system for 5-HTP, 5-HT, tryptophan, and 5-HIAA was 6.0, 7.1, 17.5, and 7.6 pg, resptively, with recovery rates of apprx 99% and intrassay relative standard deviations of <5%|An HPLC method for the determination of tryptophan and its metabolites in maternal and umbilical cord plasma is described. Chromatography was carried out on a column packed with 10 um IRICA RP-18 using as mobile phase a mixture of 0.1 M NaOAc, 0.1 M citric acid, 0.03 mM Na2EDTA, and 5-30% acetonitrile or 10-37% MeOH. Recovery range was99.0-100.7% for tryptophan and its metabolites. Interassay relative standard deviation was in the range of 1.5-5.7% for tryptophan and its metabolites. Detection limits were <150 pg/ml for 5-HTP, 177.5 pg/ml for 5-HT): 190 pg/ml for 5-HIAA, 437 pg/ml for tryptophan. The detection limits for 5-HT and 5-HIAA were sufficient for clinical determination of pregnancy. The method was applied to the determination of tryptophan and metabolites in maternal vein plasma and in umbilical artery and vein plasma.|A capillary electrophoresis method for separation and detection with time-of-flight mass spectrometry is described for tryptophan metabolites in the kynurenic pathway...|A liquid chromatographic-tandem mass spectrometric method measures 3-hydroxykynurenine and 3-hydroxyanthranilic acid in addition to tryptophan and kynurenine both intra- and extracellularly. After reversed phase HPLC separation, the compounds were detected in the MS positive multiple reaction monitoring mode...

Human Drugs -> EU pediatric investigation plans|Cosmetics -> Antistatic