Spirulina Is More Protein Rich Than Beef.

"Tryptan" redirects here. For the type of anti-migraine drug, see Triptan. For the hydrocarbon, encounter Triptane.

l-Tryptophan

Skeletal formula of L-tryptophan
brawl-and-stick model[one] space-filling model[1]
Names
IUPAC name Tryptophan or (twoS)-ii-amino-three-(iH-indol-3-yl)propanoic acid
Other names two-Amino-3-(1H-indol-3-yl)propanoic acid
Identifiers
CAS Number	73-22-3 Y
3D model (JSmol)	Interactive prototype Zwitterion: Interactive prototype
ChEBI	CHEBI:16828
ChEMBL	ChEMBL54976 Y
ChemSpider	6066 Y
DrugBank	DB00150 Y
ECHA InfoCard	100.000.723
IUPHAR/BPS	717
KEGG	D00020 Y
PubChem CID	6305
UNII	8DUH1N11BX Y
CompTox Dashboard (EPA)	DTXSID5021419
InChI InChI=1S/C11H12N2O2/c12-9(xi(14)15)five-7-6-xiii-10-4-2-one-3-8(7)10/h1-4,6,nine,13H,5,12H2,(H,14,15)/t9-/m0/s1 Y Primal: QIVBCDIJIAJPQS-VIFPVBQESA-N Y
SMILES c1[nH]c2ccccc2c1C[C@H](North)C(=O)O Zwitterion: c1[nH]c2ccccc2c1C[C@H]([NH3+])C(=O)[O-]
Backdrop
Chemical formula	C 11 H 12 N 2 O 2
Molar mass	204.229 g·mol−1
Solubility in water	Soluble: 0.23 g/L at 0 °C, xi.4 g/L at 25 °C, 17.one g/L at fifty °C, 27.95 1000/L at 75 °C
Solubility	Soluble in hot alcohol, alkali hydroxides; insoluble in chloroform.
Acidity (pM a)	ii.38 (carboxyl), 9.39 (amino)[2]
Magnetic susceptibility (χ)	-132.0·10−6 cm3/mol
Pharmacology
ATC lawmaking	N06AX02 (WHO)
Supplementary information page
Tryptophan (data page)
Except where otherwise noted, data are given for materials in their standard land (at 25 °C [77 °F], 100 kPa). Infobox references

Chemical compound

Tryptophan (symbol Trp or West)^[3] is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acrid grouping, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. Information technology is essential in humans, pregnant that the body cannot synthesize it and information technology must be obtained from the diet. Tryptophan is also a forerunner to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3.^[4] It is encoded by the codon UGG.

Similar other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (–NH ⁺
₃ ; pK_a = 9.39) and the carboxylic acrid is deprotonated ( –COO⁻; pK_a = ii.38).^[5]

Many animals (including humans) cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acrid.

Function [edit]

Metabolism of

l-tryptophan into serotonin and melatonin (left) and niacin (correct). Transformed functional groups afterward each chemical reaction are highlighted in ruddy.

Amino acids, including tryptophan, are used as edifice blocks in protein biosynthesis, and proteins are required to sustain life. Many animals (including humans) cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid. Tryptophan is among the less mutual amino acids found in proteins, but it plays important structural or functional roles whenever it occurs. For instance, tryptophan and tyrosine residues play special roles in "anchoring" membrane proteins within the cell membrane. Tryptophan, along with other aromatic amino acids, is also important in glycan-protein interactions. In addition, tryptophan functions as a biochemical precursor for the following compounds:

• Serotonin (a neurotransmitter), synthesized by tryptophan hydroxylase.^{[six] [7]}
• Melatonin (a neurohormone) is in plow synthesized from serotonin, via Due north-acetyltransferase and v-hydroxyindole-O-methyltransferase enzymes.^[8]
• Kynurenine, to which tryptophan is mainly (more than 95%) metabolized. Two enzymes, namely indoleamine 2,3-dioxygenase (IDO) in the allowed organization and the encephalon, and tryptophan 2,3-dioxygenase (TDO) in the liver, are responsible for the synthesis of kynurenine from tryptophan. The kynurenine pathway of tryptophan catabolism is altered in several diseases, including psychiatric disorders such as schizophrenia,^[9] major depressive disorder,^[ix] and bipolar disorder.^{[ix] [ten]}
• Niacin, too known as vitamin B₃, is synthesized from tryptophan via kynurenine and quinolinic acids.^[11]
• Auxins (a class of phytohormones) are synthesized from tryptophan.^[12]

The disorder fructose malabsorption causes improper assimilation of tryptophan in the intestine, reduced levels of tryptophan in the blood,^[13] and low.^[fourteen]

In leaner that synthesize tryptophan, loftier cellular levels of this amino acid activate a repressor protein, which binds to the trp operon.^[15] Binding of this repressor to the tryptophan operon prevents transcription of downstream DNA that codes for the enzymes involved in the biosynthesis of tryptophan. So high levels of tryptophan foreclose tryptophan synthesis through a negative feedback loop, and when the jail cell's tryptophan levels go down again, transcription from the trp operon resumes. This permits tightly regulated and rapid responses to changes in the cell's internal and external tryptophan levels.

Recommended dietary assart [edit]

In 2002, the U.S. Constitute of Medicine gear up a Recommended Dietary Allowance (RDA) of five mg/kg body weight/day of Tryptophan for adults 19 years and over.^[xx]

Dietary sources [edit]

Tryptophan is present in most protein-based foods or dietary proteins. It is particularly plentiful in chocolate, oats, stale dates, milk, yogurt, cottage cheese, red meat, eggs, fish, poultry, sesame, chickpeas, almonds, sunflower seeds, pumpkin seeds, Hemp Seeds, buckwheat, spirulina, and peanuts. Contrary to the popular belief^{[21] [22]} that cooked turkey contains an abundance of tryptophan, the tryptophan content in turkey is typical of poultry.^[23]

Tryptophan (Trp) content of various foods^{[23] [24]}

Nutrient	Tryptophan [1000/100 g of food]	Protein [thou/100 g of food]	Tryptophan/poly peptide [%]
Egg white, dried	1.00	81.10	1.23
Spirulina, dried	0.92	57.47	1.62
Cod, Atlantic, stale	0.lxx	62.82	1.11
Soybeans, raw	0.59	36.49	one.62
Cheese, Parmesan	0.56	37.xc	1.47
Chia seeds, stale	0.436	sixteen.5	2.64
Sesame seed	0.37	17.00	2.17
Cheese, Cheddar	0.32	24.90	1.29
Sunflower seed	0.30	17.20	1.74
Pork, chop	0.25	19.27	one.27
Turkey	0.24	21.89	ane.xi
Chicken	0.24	20.85	one.fourteen
Beefiness	0.23	20.thirteen	1.12
Oats	0.23	16.89	1.39
Salmon	0.22	xix.84	one.12
Lamb, chop	0.21	18.33	1.17
Perch, Atlantic	0.21	eighteen.62	1.12
Chickpeas, raw	0.19	19.30	0.96
Egg	0.17	12.58	ane.33
Wheat flour, white	0.thirteen	x.33	ane.23
Baking chocolate, unsweetened	0.13	12.9	1.23
Milk	0.08	three.22	2.34
Rice, white, medium-grain, cooked	0.028	ii.38	1.xviii
Quinoa, uncooked	0.167	14.12	1.2
Quinoa, cooked	0.052	iv.twoscore	1.1
Potatoes, russet	0.02	2.14	0.84
Tamarind	0.018	two.80	0.64
Banana	0.01	one.03	0.87

Medical use [edit]

Depression [edit]

Because tryptophan is converted into v-hydroxytryptophan (five-HTP) which is then converted into the neurotransmitter serotonin, it has been proposed that consumption of tryptophan or 5-HTP may meliorate depression symptoms by increasing the level of serotonin in the brain. Tryptophan is sold over the counter in the U.s. (later on being banned to varying extents between 1989 and 2005) and the U.k. as a dietary supplement for use as an antidepressant, anxiolytic, and sleep help. It is also marketed equally a prescription drug in some European countries for the handling of major low. There is evidence that blood tryptophan levels are unlikely to be altered by changing the nutrition,^{[25] [26]} but consuming purified tryptophan increases the serotonin level in the brain, whereas eating foods containing tryptophan does not.^[27]

In 2001 a Cochrane review of the effect of 5-HTP and tryptophan on low was published. The authors included only studies of a high rigor and included both 5-HTP and tryptophan in their review considering of the limited data on either. Of 108 studies of 5-HTP and tryptophan on depression published between 1966 and 2000, merely two met the authors' quality standards for inclusion, totaling 64 report participants. The substances were more effective than placebo in the two studies included but the authors state that "the evidence was of insufficient quality to exist conclusive" and annotation that "considering alternative antidepressants exist which have been proven to be effective and safe, the clinical usefulness of 5-HTP and tryptophan is limited at present".^[28] The use of tryptophan as an adjunctive therapy in addition to standard treatment for mood and anxiety disorders is not supported by the scientific bear witness.^{[28] [29]}

Insomnia [edit]

The American University of Sleep Medicine'south 2017 clinical practice guidelines recommended against the utilize of tryptophan in the treatment of insomnia due to poor effectiveness.^[30]

Side effects [edit]

Potential side effects of tryptophan supplementation include nausea, diarrhea, drowsiness, lightheadedness, headache, dry mouth, blurred vision, sedation, euphoria, and nystagmus (involuntary eye movements).^{[31] [32]}

Interactions [edit]

Tryptophan taken as a dietary supplement (such as in tablet form) has the potential to cause serotonin syndrome when combined with antidepressants of the MAOI or SSRI course or other strongly serotonergic drugs.^[32] Considering tryptophan supplementation has not been thoroughly studied in a clinical setting, its interactions with other drugs are non well known.^[28]

Isolation [edit]

The isolation of tryptophan was offset reported by Frederick Hopkins in 1901.^[33] Hopkins recovered tryptophan from hydrolysed casein, recovering 4–8 1000 of tryptophan from 600 g of rough casein.^[34]

Biosynthesis and industrial production [edit]

As an essential amino acid, tryptophan is not synthesized from simpler substances in humans and other animals, so information technology needs to be nowadays in the nutrition in the class of tryptophan-containing proteins. Plants and microorganisms commonly synthesize tryptophan from shikimic acid or anthranilate:^[35] anthranilate condenses with phosphoribosylpyrophosphate (PRPP), generating pyrophosphate equally a past-production. The ring of the ribose moiety is opened and subjected to reductive decarboxylation, producing indole-3-glycerol phosphate; this, in turn, is transformed into indole. In the last step, tryptophan synthase catalyzes the formation of tryptophan from indole and the amino acrid serine.

The industrial production of tryptophan is too biosynthetic and is based on the fermentation of serine and indole using either wild-type or genetically modified leaner such every bit B. amyloliquefaciens, B. subtilis, C. glutamicum or E. coli. These strains carry mutations that foreclose the reuptake of aromatic amino acids or multiple/overexpressed trp operons. The conversion is catalyzed by the enzyme tryptophan synthase.^{[36] [37] [38]}

Social club and civilisation [edit]

Showa Denko contamination scandal [edit]

There was a large outbreak of eosinophilia-myalgia syndrome (European monetary system) in the U.South. in 1989, with more than 1,500 cases reported to the CDC and at least 37 deaths.^[39] Afterwards preliminary investigation revealed that the outbreak was linked to intake of tryptophan, the U.S. Food and Drug Administration (FDA) recalled tryptophan supplements in 1989 and banned most public sales in 1990,^{[forty] [41] [42]} with other countries post-obit arrange.^{[43] [44]}

Subsequent studies suggested that EMS was linked to specific batches of L-tryptophan supplied past a single large Japanese manufacturer, Showa Denko.^{[40] [45] [46] [47]} It eventually became clear that recent batches of Showa Denko's L-tryptophan were contaminated by trace impurities, which were after thought to be responsible for the 1989 EMS outbreak.^{[40] [48] [49]} However, other testify suggests that tryptophan itself may be a potentially major contributory factor in EMS.^[50] There are also claims that a precursor reached sufficient concentrations to form a toxic dimer^[51]

The FDA loosened its restrictions on sales and marketing of tryptophan in February 2001,^[xl] just continued to limit the importation of tryptophan not intended for an exempted employ until 2005.^[52]

The fact that the Showa Denko facility used genetically engineered leaner to produce the contaminated batches of L-tryptophan later constitute to have caused the outbreak of eosinophilia-myalgia syndrome has been cited every bit prove of a need for "close monitoring of the chemical purity of biotechnology-derived products".^[53] Those calling for purity monitoring have, in plow, been criticized every bit anti-GMO activists who overlook possible non-GMO causes of contamination and threaten the development of biotech.^[54]

Turkey meat and drowsiness hypothesis [edit]

A common exclamation in the U.s.a. is that heavy consumption of turkey meat results in drowsiness, due to high levels of tryptophan contained in turkey.^[22] Nonetheless, the amount of tryptophan in turkey is comparable to that contained in other meats.^{[21] [23]} Drowsiness later on eating may be caused by other foods eaten with the turkey, particularly carbohydrates.^[55] Ingestion of a repast rich in carbohydrates triggers the release of insulin.^{[56] [57] [58] [59]} Insulin in plough stimulates the uptake of large neutral branched-chain amino acids (BCAA), but not tryptophan, into musculus, increasing the ratio of tryptophan to BCAA in the claret stream. The resulting increased tryptophan ratio reduces contest at the large neutral amino acid transporter (which transports both BCAA and aromatic amino acids), resulting in more than uptake of tryptophan across the blood–brain bulwark into the cerebrospinal fluid (CSF).^{[59] [60] [61]} Once in the CSF, tryptophan is converted into serotonin in the raphe nuclei by the normal enzymatic pathway.^{[57] [62]} The resultant serotonin is farther metabolised into melatonin by the pineal gland.^[8] Hence, these information advise that "feast-induced drowsiness"—or postprandial somnolence—may be the result of a heavy meal rich in carbohydrates, which indirectly increases the production of melatonin in the encephalon, and thereby promotes sleep.^{[56] [57] [58] [62]}

Enquiry [edit]

In 1912 Felix Ehrlich demonstrated that yeast metabolizes the natural amino acids substantially by splitting off carbon dioxide and replacing the amino group with a hydroxyl grouping. By this reaction, tryptophan gives rise to tryptophol.^[63]

Tryptophan affects encephalon serotonin synthesis when given orally in a purified course and is used to modify serotonin levels for research.^[27] Low encephalon serotonin level is induced by administration of tryptophan-poor poly peptide in a technique called acute tryptophan depletion.^[64] Studies using this method have evaluated the effect of serotonin on mood and social behavior, finding that serotonin reduces aggression and increases agreeableness.^[65]

Fluorescence [edit]

Tryptophan is an important intrinsic fluorescent probe (amino acrid), which tin can exist used to estimate the nature of the microenvironment around the tryptophan balance. Most of the intrinsic fluorescence emissions of a folded protein are due to excitation of tryptophan residues.

See also [edit]

• 5-Hydroxytryptophan (v-HTP)
• Acree–Rosenheim reaction
• Adamkiewicz reaction
• Attenuator (genetics)
• N,Northward-Dimethyltryptamine
• Hopkins–Cole reaction
• Serotonin
• Tryptamine

References [edit]

1. ^ ^{a b} Görbitz, C. H.; Törnroos, Thousand. W.; Day, Yard. Chiliad. (2012). "Single-crystal investigation of L-tryptophan with Z′ = 16". Acta Crystallogr. B. 68 (Pt five): 549–557. doi:ten.1107/S0108768112033484. PMID 22992800.
2. ^ Dawson RM, et al. (1969). Data for Biochemical Research . Oxford: Clarendon Press. ISBN0-nineteen-855338-ii.
3. ^ "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on nine Oct 2008. Retrieved 5 March 2018.
4. ^ Slominski A, Semak I, Pisarchik A, Sweatman T, Szczesniewski A, Wortsman J (2002). "Conversion of L-tryptophan to serotonin and melatonin in human being melanoma cells". FEBS Letters. 511 (one–3): 102–vi. doi:10.1016/s0014-5793(01)03319-i. PMID 11821057. S2CID 7820568.
5. ^ "L-tryptophan | C11H12N2O2 - PubChem". pubchem.ncbi.nlm.nih.gov . Retrieved 22 Dec 2016.
6. ^ Fernstrom JD (1983). "Role of forerunner availability in control of monoamine biosynthesis in brain". Physiological Reviews. 63 (2): 484–546. doi:10.1152/physrev.1983.63.2.484. PMID 6132421.
7. ^ Schaechter JD, Wurtman RJ (1990). "Serotonin release varies with encephalon tryptophan levels" (PDF). Brain Research. 532 (1–ii): 203–ten. doi:x.1016/0006-8993(90)91761-v. PMID 1704290. S2CID 8451316.
8. ^ ^{a b} Wurtman RJ, Anton-Tay F (1969). "The mammalian pineal as a neuroendocrine transducer" (PDF). Recent Progress in Hormone Research. 25: 493–522. doi:10.1016/b978-0-12-571125-eight.50014-4. ISBN9780125711258. PMID 4391290. Archived from the original (PDF) on 31 May 2014.
9. ^ ^{a b c} Marx, Wolfgang; McGuinness, Amelia J.; Rocks, Tetyana; Ruusunen, Anu; Cleminson, Jasmine; Walker, Adam J.; Gomes-da-Costa, Susana; Lane, Melissa; Sanches, Marsal; Diaz, Alexandre P.; Tseng, Ping-Tao (23 Nov 2020). "The kynurenine pathway in major depressive disorder, bipolar disorder, and schizophrenia: a meta-analysis of 101 studies". Molecular Psychiatry. 26 (viii): 4158–4178. doi:10.1038/s41380-020-00951-9. ISSN 1476-5578. PMID 33230205. S2CID 227132820.
10. ^ Bartoli, F; Misiak, B; Callovini, T; Cavaleri, D; Cioni, RM; Crocamo, C; Savitz, JB; Carrà, Thousand (19 October 2020). "The kynurenine pathway in bipolar disorder: a meta-analysis on the peripheral blood levels of tryptophan and related metabolites". Molecular Psychiatry. 26 (7): 3419–3429. doi:x.1038/s41380-020-00913-one. PMID 33077852. S2CID 224314102.
11. ^ Ikeda G, Tsuji H, Nakamura South, Ichiyama A, Nishizuka Y, Hayaishi O (1965). "Studies on the biosynthesis of nicotinamide adenine dinucleotide. II. A office of picolinic carboxylase in the biosynthesis of nicotinamide adenine dinucleotide from tryptophan in mammals". The Journal of Biological Chemistry. 240 (iii): 1395–401. doi:10.1016/S0021-9258(18)97589-vii. PMID 14284754.
12. ^ Palme K, Nagy F (2008). "A new cistron for auxin synthesis". Jail cell. 133 (1): 31–2. doi:10.1016/j.cell.2008.03.014. PMID 18394986. S2CID 9949830.
13. ^ Ledochowski M, Widner B, Murr C, Sperner-Unterweger B, Fuchs D (2001). "Fructose malabsorption is associated with decreased plasma tryptophan" (PDF). Scandinavian Journal of Gastroenterology. 36 (iv): 367–71. doi:10.1080/003655201300051135. PMID 11336160. Archived from the original (PDF) on 19 April 2016.
14. ^ Ledochowski M, Sperner-Unterweger B, Widner B, Fuchs D (June 1998). "Fructose malabsorption is associated with early signs of mental depression". European Periodical of Medical Research. three (six): 295–8. PMID 9620891.
15. ^ Gollnick P, Babitzke P, Antson A, Yanofsky C (2005). "Complication in regulation of tryptophan biosynthesis in Bacillus subtilis". Annual Review of Genetics. 39: 47–68. doi:10.1146/annurev.genet.39.073003.093745. PMID 16285852.
16. ^ ^{a b c d e f 1000 h i} Zhang LS, Davies SS (Apr 2016). "Microbial metabolism of dietary components to bioactive metabolites: opportunities for new therapeutic interventions". Genome Med. viii (1): 46. doi:10.1186/s13073-016-0296-10. PMC4840492. PMID 27102537. Lactobacillus spp. convert tryptophan to indole-three-aldehyde (I3A) through unidentified enzymes [125]. Clostridium sporogenes convert tryptophan to IPA [6], probable via a tryptophan deaminase. ... IPA also potently scavenges hydroxyl radicals
    Table 2: Microbial metabolites: their synthesis, mechanisms of activity, and effects on health and illness
    Figure 1: Molecular mechanisms of action of indole and its metabolites on host physiology and disease
17. ^ Wikoff WR, Anfora AT, Liu J, Schultz PG, Lesley SA, Peters EC, Siuzdak G (March 2009). "Metabolomics analysis reveals large effects of gut microflora on mammalian blood metabolites". Proc. Natl. Acad. Sci. The statesA. 106 (x): 3698–3703. Bibcode:2009PNAS..106.3698W. doi:x.1073/pnas.0812874106. PMC2656143. PMID 19234110. Production of IPA was shown to be completely dependent on the presence of gut microflora and could exist established by colonization with the bacterium Clostridium sporogenes.
    IPA metabolism diagram
18. ^ "3-Indolepropionic acid". Human Metabolome Database. University of Alberta. Retrieved 12 June 2018.
19. ^ Chyan YJ, Poeggeler B, Omar RA, Chain DG, Frangione B, Ghiso J, Pappolla MA (July 1999). "Potent neuroprotective properties against the Alzheimer beta-amyloid by an endogenous melatonin-related indole structure, indole-3-propionic acid". J. Biol. Chem. 274 (31): 21937–21942. doi:10.1074/jbc.274.31.21937. PMID 10419516. S2CID 6630247. [Indole-iii-propionic acid (IPA)] has previously been identified in the plasma and cerebrospinal fluid of humans, merely its functions are non known. ... In kinetic competition experiments using free radical-trapping agents, the chapters of IPA to scavenge hydroxyl radicals exceeded that of melatonin, an indoleamine considered to exist the most potent naturally occurring scavenger of free radicals. In contrast with other antioxidants, IPA was not converted to reactive intermediates with pro-oxidant activeness.
20. ^ Establish of Medicine (2002). "Protein and Amino Acids". Dietary Reference Intakes for Free energy, Carbohydrates, Cobweb, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids. Washington, DC: The National Academies Press. pp. 589–768. doi:10.17226/10490. ISBN978-0-309-08525-0.
21. ^ ^{a b} Ballantyne C (21 Nov 2007). "Does Turkey Brand You Sleepy?". Scientific American . Retrieved vi June 2013.
22. ^ ^{a b} McCue G. "Chemistry.org: Thanksgiving, Turkey, and Tryptophan". Archived from the original on 4 April 2007. Retrieved 17 August 2007.
23. ^ ^{a b c} Holden, Joanne. "USDA National Nutrient Database for Standard Reference, Release 22". Food Information Laboratory, Agricultural Research Service, Us Department of Agriculture. Retrieved 29 Nov 2009.
24. ^ Rambali B, Van Andel I, Schenk E, Wolterink G, van de Werken G, Stevenson H, Vleeming W (2002). "[The contribution of cocoa additive to cigarette smoking addiction]" (PDF). RIVM. The National Plant for Public Health and the Environment (Netherlands) (report 650270002/2002). Archived from the original (PDF) on 8 Nov 2005.
25. ^ Soh NL, Walter GT (2011). "Tryptophan and low: can diet alone be the answer?". Acta Neuropsychiatrica. 23 (ane): 1601–5215. doi:ten.1111/j.1601-5215.2010.00508.ten. S2CID 145779393.
26. ^ Fernstrom JD (2012). "Effects and side effects associated with the non-nutritional utilize of tryptophan by humans". The Journal of Nutrition. 142 (12): 2236S–2244S. doi:ten.3945/jn.111.157065. PMID 23077193.
27. ^ ^{a b} Wurtman RJ, Hefti F, Melamed Eastward (1980). "Precursor command of neurotransmitter synthesis". Pharmacological Reviews. 32 (4): 315–35. PMID 6115400.
28. ^ ^{a b c} Shaw K, Turner J, Del Mar C (2002). Shaw KA (ed.). "Tryptophan and 5-hydroxytryptophan for depression" (PDF). The Cochrane Database of Systematic Reviews. 2010 (i): CD003198. doi:10.1002/14651858.CD003198. PMID 11869656.
29. ^ Ravindran AV, da Silva TL (September 2013). "Complementary and culling therapies equally add-on to pharmacotherapy for mood and feet disorders: a systematic review". Journal of Affective Disorders. 150 (3): 707–nineteen. doi:10.1016/j.jad.2013.05.042. PMID 23769610.
30. ^ Sateia MJ, Buysse DJ, Krystal AD, Neubauer DN, Heald JL (February 2017). "Clinical Practice Guideline for the Pharmacologic Handling of Chronic Insomnia in Adults: An American University of Sleep Medicine Clinical Practise Guideline". J Clin Sleep Med. 13 (2): 307–349. doi:10.5664/jcsm.6470. PMC5263087. PMID 27998379.
31. ^ Kimura T, Bier DM, Taylor CL (Dec 2012). "Summary of workshop discussions on establishing upper limits for amino acids with specific attention to available data for the essential amino acids leucine and tryptophan". The Journal of Nutrition. 142 (12): 2245S–2248S. doi:10.3945/jn.112.160846. PMID 23077196.
32. ^ ^{a b} Howland RH (June 2012). "Dietary supplement drug therapies for depression". Periodical of Psychosocial Nursing and Mental Wellness Services. fifty (6): thirteen–half dozen. doi:10.3928/02793695-20120508-06. PMID 22589230.
33. ^ Hopkins FG, Cole SW (December 1901). "A contribution to the chemical science of proteids: Function I. A preliminary written report of a hitherto undescribed product of tryptic digestion". The Journal of Physiology. 27 (iv–v): 418–428. doi:10.1113/jphysiol.1901.sp000880. PMC1540554. PMID 16992614.
34. ^ Cox, G.J.; King, H. (1930). "L-Tryptophane". Org. Synth. 10: 100. doi:10.15227/orgsyn.010.0100.
35. ^ Radwanski ER, Last RL (1995). "Tryptophan biosynthesis and metabolism: biochemical and molecular genetics". The Plant Jail cell. 7 (7): 921–34. doi:10.1105/tpc.7.seven.921. PMC160888. PMID 7640526.
36. ^ Ikeda 1000 (2002). "Amino acrid production processes". Microbial Production of fifty-Amino Acids. Advances in Biochemical Engineering science/Biotechnology. Vol. 79. pp. ane–35. doi:10.1007/three-540-45989-8_1. ISBN978-3-540-43383-5. PMID 12523387.
37. ^ Becker J, Wittmann C (2012). "Bio-based production of chemicals, materials and fuels -Corynebacterium glutamicum equally versatile cell manufacturing plant". Current Opinion in Biotechnology. 23 (4): 631–40. doi:10.1016/j.copbio.2011.xi.012. PMID 22138494.
38. ^ Conrado RJ, Varner JD, DeLisa MP (2008). "Technology the spatial system of metabolic enzymes: mimicking nature'due south synergy". Electric current Opinion in Biotechnology. 19 (v): 492–9. doi:10.1016/j.copbio.2008.07.006. PMID 18725290.
39. ^ Allen, J.A.; Varga, J (2014). "Eosinophilia–Myalgia Syndrome". In Wexler, Philip (ed.). Encyclopedia of Toxicology (3rd ed.). Burlington: Elsevier Scientific discipline. ISBN978-0-12-386455-0.
40. ^ ^{a b c d} "Information Paper on 50-tryptophan and five-hydroxy-L-tryptophan". FU. S. Nutrient and Drug Administration, Center for Food Rubber and Applied Nutrition, Office of Nutritional Products, Labeling, and Dietary Supplements. 1 February 2001. Archived from the original on 25 Feb 2005. Retrieved viii Feb 2012.
41. ^ "L-tryptophan: Uses and Risks". WebMD. 12 May 2017. Retrieved 5 June 2017.
42. ^ Altman, Lawrence K. (27 April 1990). "Studies Tie Disorder to Maker of Food Supplement". The New York Times.
43. ^ Castot, A; Bidault, I; Bournerias, I; Carlier, P; Efthymiou, ML (1991). "["Eosinophilia-myalgia" syndrome due to L-tryptophan containing products. Cooperative evaluation of French Regional Centers of Pharmacovigilance. Analysis of 24 cases]". Thérapie. 46 (5): 355–65. PMID 1754978.
44. ^ "COT Statement on Tryptophan and the Eosinophilia-Myalgia Syndrome" (PDF). United kingdom Committee on Toxicity of Chemicals in Nutrient, Consumer Products and the Environment. June 2004.
45. ^ Slutsker Fifty, Hoesly FC, Miller Fifty, Williams LP, Watson JC, Fleming DW (July 1990). "Eosinophilia-myalgia syndrome associated with exposure to tryptophan from a single manufacturer". JAMA. 264 (two): 213–vii. doi:10.1001/jama.264.ii.213. PMID 2355442.
46. ^ Back EE, Henning KJ, Kallenbach LR, Brix KA, Gunn RA, Melius JM (April 1993). "Risk factors for developing eosinophilia myalgia syndrome amid Fifty-tryptophan users in New York". The Journal of Rheumatology. twenty (iv): 666–72. PMID 8496862.
47. ^ Kilbourne EM, Philen RM, Kamb ML, Falk H (October 1996). "Tryptophan produced by Showa Denko and epidemic eosinophilia-myalgia syndrome". The Journal of Rheumatology. Supplement. 46: 81–eight, discussion 89–91. PMID 8895184.
48. ^ Mayeno AN, Lin F, Foote CS, Loegering DA, Ames MM, Hedberg CW, Gleich GJ (December 1990). "Characterization of "elevation E," a novel amino acid associated with eosinophilia-myalgia syndrome". Science. 250 (4988): 1707–8. Bibcode:1990Sci...250.1707M. doi:10.1126/scientific discipline.2270484. PMID 2270484.
49. ^ Ito J, Hosaki Y, Torigoe Y, Sakimoto Thou (January 1992). "Identification of substances formed past decomposition of peak E substance in tryptophan". Food and Chemic Toxicology. 30 (1): 71–81. doi:10.1016/0278-6915(92)90139-C. PMID 1544609.
50. ^ Smith MJ, Garrett RH (November 2005). "A heretofore undisclosed crux of eosinophilia-myalgia syndrome: compromised histamine deposition". Inflammation Enquiry. 54 (11): 435–l. doi:10.1007/s00011-005-1380-7. PMID 16307217. S2CID 7785345.
51. ^ Michael Predator Carlton. "Molecular Biology and Genetic Engineering explained by someone who's done it". Archived from the original on 24 June 2007.
52. ^ Allen, JA; Peterson, A; Sufit, R; Hinchcliff, ME; Mahoney, JM; Wood, TA; Miller, FW; Whitfield, ML; Varga, J (November 2011). "Post-epidemic eosinophilia-myalgia syndrome associated with L-tryptophan". Arthritis and Rheumatism. 63 (11): 3633–ix. doi:ten.1002/art.30514. PMC3848710. PMID 21702023.
53. ^ Mayeno AN, Gleich GJ (September 1994). "Eosinophilia-myalgia syndrome and tryptophan production: a cautionary tale". Trends in Biotechnology. 12 (ix): 346–52. doi:ten.1016/0167-7799(94)90035-3. PMID 7765187.
54. ^ Raphals P (November 1990). "Does medical mystery threaten biotech?". Science. 250 (4981): 619. Bibcode:1990Sci...250..619R. doi:10.1126/science.2237411. PMID 2237411.
55. ^ "Food & mood. (neuroscience professor Richard Wurtman) (Interview)". Nutrition Action Healthletter. September 1992. ^{[ dead link ]}
56. ^ ^{a b} Lyons PM, Truswell AS (March 1988). "Serotonin precursor influenced by blazon of saccharide repast in salubrious adults". The American Journal of Clinical Nutrition. 47 (3): 433–9. doi:10.1093/ajcn/47.iii.433. PMID 3279747.
57. ^ ^{a b c} Wurtman RJ, Wurtman JJ, Regan MM, McDermott JM, Tsay RH, Breu JJ (January 2003). "Furnishings of normal meals rich in carbohydrates or proteins on plasma tryptophan and tyrosine ratios". The American Journal of Clinical Nutrition. 77 (one): 128–32. doi:x.1093/ajcn/77.1.128. PMID 12499331.
58. ^ ^{a b} Afaghi A, O'Connor H, Chow CM (February 2007). "High-glycemic-index carbohydrate meals shorten sleep onset". The American Journal of Clinical Nutrition. 85 (2): 426–30. doi:ten.1093/ajcn/85.2.426. PMID 17284739.
59. ^ ^{a b} Banks WA, Owen JB, Erickson MA (2012). "Insulin in the Brain: There and Back Again". Pharmacology & Therapeutics. 136 (1): 82–93. doi:10.1016/j.pharmthera.2012.07.006. ISSN 0163-7258. PMC4134675. PMID 22820012.
60. ^ Pardridge WM, Oldendorf WH (August 1975). "Kinetic analysis of blood-brain bulwark transport of amino acids". Biochimica et Biophysica Acta (BBA) - Biomembranes. 401 (1): 128–36. doi:10.1016/0005-2736(75)90347-8. PMID 1148286.
61. ^ Maher TJ, Glaeser BS, Wurtman RJ (May 1984). "Diurnal variations in plasma concentrations of bones and neutral amino acids and in red cell concentrations of aspartate and glutamate: effects of dietary protein intake". The American Journal of Clinical Nutrition. 39 (5): 722–ix. doi:x.1093/ajcn/39.five.722. PMID 6538743.
62. ^ ^{a b} Fernstrom JD, Wurtman RJ (1971). "Brain serotonin content: increase post-obit ingestion of sugar diet". Science. 174 (4013): 1023–5. Bibcode:1971Sci...174.1023F. doi:10.1126/science.174.4013.1023. PMID 5120086. S2CID 14345137.
63. ^ Jackson RW (1930). "A synthesis of tryptophol" (PDF). Journal of Biological Chemistry. 88 (three): 659–662. doi:x.1016/S0021-9258(eighteen)76755-0.
64. ^ Young SN (September 2013). "Astute tryptophan depletion in humans: a review of theoretical, practical and ethical aspects". Journal of Psychiatry & Neuroscience. 38 (v): 294–305. doi:x.1503/jpn.120209. PMC3756112. PMID 23428157.
65. ^ Young SN (2013). "The effect of raising and lowering tryptophan levels on human mood and social behaviour". Philosophical Transactions of the Royal Club of London. Serial B, Biological Sciences. 368 (1615): 20110375. doi:10.1098/rstb.2011.0375. PMC3638380. PMID 23440461.

Further reading [edit]

• Wood RM, Rilling JK, Sanfey AG, Bhagwagar Z, Rogers RD (May 2006). "Effects of tryptophan depletion on the performance of an iterated Prisoner'south Dilemma game in good for you adults". Neuropsychopharmacology. 31 (v): 1075–84. doi:10.1038/sj.npp.1300932. PMID 16407905.

External links [edit]

• "KEGG PATHWAY: Tryptophan metabolism - Man sapiens". KEGG: Kyoto Encyclopedia of Genes and Genomes. 23 August 2006. Retrieved 20 April 2008.
• G. P. Moss. "Tryptophan Catabolism (early stages)". Nomenclature Committee of the International Matrimony of Biochemistry and Molecular Biology (NC-IUBMB). Archived from the original on thirteen September 2003. Retrieved twenty April 2008.
• G. P. Moss. "Tryptophan Catabolism (later stages)". Classification Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Archived from the original on 13 September 2003. Retrieved xx April 2008.
• B. Mikkelson; D. P. Mikkelson (22 Nov 2007). "Turkey Causes Sleepiness". Urban Legends Reference Pages. Snopes.com. Retrieved 20 Apr 2008.

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Source: https://en.wikipedia.org/wiki/Tryptophan

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