L-Phenylalanine

165.18900

165.19

200-568-1

47E5O17Y3R

DTXSID4040763

C29601

Prisms form water|Monoclinic plates, leaflets from warm concentrated aqueous solution; hydrated needles from dilute solutions

29224995

63.32000

1.34130

L-phenylalanine is an odorless white crystalline powder. Slightly bitter taste. pH (1% aqueous solution) 5.4 to 6. (NTP, 1992)

1.24 g/cm³

283 °C (decomp)

307.5ºC at 760 mmHg

139.8ºC

1.576

1-5 g/100 mL at 25 ºC

Store at RT.

<1 Pa (25 °C)

Specific optical rotation: -35.1 deg at 20 °C/D (c = 1.94)

Slight

Bitter

1.24(at 25 °C)

Henry's Law constant = 1.2X10-10 atm-cu m/mol at 25 °C (est)

1.24 (at 25 °C)|pK1 = 1.83; pK2 = 9.13|pKa = 1.24

140.3 Ų [M+H]+ [CCS Type: DT, Method: single field calibrated with Agilent tune mix (Agilent)]|138.91 Ų [M+Na]+ [CCS Type: DT, Method: stepped-field]|146.52 Ų [M-H]- [CCS Type: DT, Method: stepped-field]|135 Ų [M+H]+ [CCS Type: TW, Method: calibrated with polyalanine]|140.2 Ų [M+H]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|138.3 Ų [M+Na]+ [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|139.4 Ų [M-H]- [CCS Type: DT, Method: single field calibrated with ESI Low Concentration Tuning Mix (Agilent)]|141.29 Ų [M-H]- [CCS Type: DT, Method: stepped-field]|141.28 Ų [M+H]+ [CCS Type: DT, Method: stepped-field]|140.1 Ų [M-H]-

Sublimes in vacuo|Leaflets from water, decomposes at 285 °C. Specfic optical rotation: +35.0 deg at 20 °C/D (c = 2.04); +7.1 deg at 20 °C/D (c = 3.8 in 18% HCl). One gram dissolves in 35.5 mL water at 16 °C. Sparingly soluble in methanol /Phenylalanine D-form/|OCCURS IN ISOMERIC FORMS /PHENYLALANINE/

Water soluble. Aqueous solutions are weak acids.

Salts, Acidic

L-PHENYLALANINE may be light sensitive. Acts as a weak acid in solution.

NONH for all modes of transport

3

R36/37/38

S22; S24/25; S37/39; S45; S36/37/39; S27; S26

AY7535000

C

Stable. Incompatible with strong oxidizing agents.

P261, P264, P271, P280, P304+P340, P305+P351+P338, P312, P337+P313, P403+P233, P405, P501

H319

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-Phenylalanine 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: phenylalanine is included in weight control drug products.|Phenylalanine used as a nutrient and/or dietary supplement in animal drugs, feeds, and related products is generally recognized as safe when used in accordance with good manufacturing or feeding practice.

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]

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

|Warning|H319 (100%): Causes serious eye irritation [Warning Serious eye damage/eye irritation]|P264, P280, P305+P351+P338, and P337+P313|Aggregated GHS information provided by 261 companies from 5 notifications to the ECHA C&L Inventory.

Fires involving this material can be controlled with 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 protect this material from exposure to light, and store it at ambient temperatures. (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)

(L)-Phenylalanine was detected in horizontal soil barriers in an active landfill, Conica-Montemarta, Sevilla, South Spain, in a low permeability clay soil. The compound was present at 5.3, and 8.4 and 11.4 nmol/g at 1-1.5 meters, 3-3.5 meters, and 6.5-7 meters depth, respectively, following 2 years deposition(1).(L)-Phenylalanine has been identified as a disinfection by-product of dichloroacetonitrile, using kynurenine as a model compound for 3 naturally-occurring substances and 37 nitrogen compounds normally found in excrement(2).

Aromatic compounds are produced by bacteria, fungi and molds associated with "sick building syndrome"; phenylalanine may give rise to 2-phenylethanol, the source of the parent compound being microbial transformation of compounds present in building materials(1). Phenylalanine has been implicated as a possible source of odor in drinking water in Paris France, as a result of chlorination(2).

L-phenylalanine will exacerbate symptoms of phenylketonuria if used by phenylketonurics. L-phenylalanine was reported to exacerbate tardive dyskinesia when used by some with schizophrenia.

Ochratoxin A (0.8 mg) injected ip together with 0.8 mg of phenylalanine, 97% of animals survived, and 100% survived when 1 mg of phenylalanine was injected.

LD50 Rat ip 5287 mg/kg

Phenylketonuria (PKU) is a genetic disorder that impairs phenylalanine hydroxylase (PAH) activity. Impaired PAH activity allows phenylalanine or its catabolic byproducts to accumulate above normal levels in the plasma during critical periods of brain development. Persistently elevated levels of L-phenylalanine in the plasma before and during infancy and childhood can result in irreversible brain damage, growth retardation, and dermatologic abnormalities if dietary phenylalanine is not restricted within 1 month of birth and continued at least through childhood and adolescence. Restriction of phenylalanine intake throughout life in PKU patients is necessary to keep plasma phenylalanine levels low and to promote normal growth and brain development. If PKU is detected early and treated effectively through strict metabolic control, infants can live a normal life-span. In the United States, approximately 1 of every 15,000 infants is born with PKU.

Phenylalanine is an essential aromatic amino acid and is a precursor of melanin, dopamine, noradrenalin, and thyroxine(1). It is one of the nine indispensable amino acids that cannot be synthesized to meet body needs in animals and therefore must be provided in the diet(2). Originally isolated from the spouts of lupine(3), phenylalanine is present in the seeds and sprouts of many plants including sunflowers, spinach, peanuts and many varieties of beans(4).

(L)-Penylalanine's production and use in medicine and as a sweetener(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 54(SRC), determined from a log Kow of -1.38(2) and a regression-derived equation(3), indicates that (L)-phenylalanine is expected to have high mobility in soil(SRC). Amino acids are ionic over the entire pH range and tend to be cationic in acidic media, zwitterionic in neutral media, and anioic in basic media(4). The pKa values of (L)-phenylalanine are 1.83 and 9.13(5), indicating that this compound will exist almost entirely in the ion form in the environment. Volatilization from moist soil is not expected because the acid exists as an ion and ions do not volatilize. (L)-Phenylalanine is not expected to volatilize from dry soil surfaces(SRC) based upon an estimated vapor pressure of 1.76X10-8 mm Hg at 25 °C(SRC), determined from a fragment constant method(6). Oxygen uptake was measured at 145 mg/L O2 over 3 hours in the Warburg test(7), indicating that biodegradation may be an important environmental fate process in soil(SRC).|AQUATIC FATE: Based on a classification scheme(1), an estimated Koc value of 54(SRC), determined from a log Kow of -1.38(2) and a regression-derived equation(3), indicates that (L)-phenylalanine is not expected to adsorb to suspended solids and sediment(SRC). Amino acids are ionic over the entire pH range and tend to be cationic in acidic media, zwitterionic in neutral media, and anioic in basic media(4). Measured pKa values of 1.83 and 9.13(5) indicate (L)-phenylalanine will exist almost entirely in the ion form at pH values of 5 to 9 and therefore volatilization from water surfaces is not expected to be an important fate process(6). According to a classification scheme(7), an estimated BCF of 3(SRC), from its log Kow(2) and a regression-derived equation(3), suggests the potential for bioconcentration in aquatic organisms is low(SRC). Oxygen uptake was measured at 145 mg/L O2 over 3 hours in the Warburg test(8), indicating that biodegradation may 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)-phenylalanine, which has an estimated vapor pressure of 1.76X10-8 mm Hg at 25 °C(SRC), determined from a fragment constant method(2), will exist in both the vapor and particulate phases in the ambient atmosphere. Vapor-phase (L)-phenylalanine is degraded in the atmosphere by reaction with photochemically-produced hydroxyl radicals(SRC); the half-life for this reaction in air is estimated to be 8.7 hours(SRC), calculated from its rate constant of 4.42X10-11 cu cm/molecule-sec at 25 °C(SRC) that was derived using a structure estimation method(3). Particulate-phase (L)-phenylalanine may be removed from the air by wet or dry deposition(SRC). (L)-Phenylalanine does not contain chromophores that absorb at wavelengths >290 nm(4), and therefore is not expected to be susceptible to direct photolysis by sunlight(SRC).

The rate constant for the vapor-phase reaction of (L)-phenylalanine with photochemically-produced hydroxyl radicals has been estimated as 4.42X10-11 cu cm/molecule-sec at 25 °C(SRC) using a structure estimation method(1). This corresponds to an atmospheric half-life of about 8.7 hours at an atmospheric concentration of 5X10+5 hydroxyl radicals per cu cm(1). Amino acids are ionic over the entire pH range and tend to be cationic in acidic media, zwitterionic in neutral media, and anioic in basic media(2). (L)-Phenylalanine is expected to undergo hydrolysis in the environment due to the presence of functional groups that hydrolyze under environmental conditions(3). (L)-Phenylalanine does not contain chromophores that absorb at wavelengths >290 nm(3), and therefore is not expected to be susceptible to direct photolysis by sunlight(SRC). The compound, present at 0.07 mM, did not exhibit photooxidation activity when irradiated with UV light for 50 hours in natural waters from the various regions in California and Hawaii(4).

An estimated BCF of 3 was calculated in fish for (L)-phenylalanine(SRC), using a log Kow of -1.38(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)-phenylalanine is estimated as 54(SRC), using a log Kow of -1.38(1) and a regression-derived equation(2). According to a classification scheme(3), this estimated Koc value suggests that (L)-phenylalanine is expected to have high mobility in soil. Amino acids are ionic over the entire pH range and tend to be cationic in acidic media, zwitterionic in neutral media, and anioic in basic media(4). The measured pKa1 and pKa2 values for (L)-phenylalanine are 1.83 and 9.13, respectively(5), indicating that this compound will almost entirely exist in the ion form in the environment.

Amino acids are ionic over the entire pH range and tend to be cationic in acidic media, zwitterionic in neutral media, and anioic in basic media(1). The measured pKa1 and pKa2 values for (L)-phenylalanine are 1.83 and 9.13, respectively(2), indicating that this compound will exist almost entirely in the ion form at pH values of 5 to 9 and therefore volatilization from water surfaces or moist soil is not expected to be an important fate process(3). (L)-Phenylalanine is not expected to volatilize from dry soil surfaces(SRC) based upon an estimated vapor pressure of 1.76X10-8 mm Hg(SRC), determined from a fragment constant method(4).

SURFACE WATER: (L)-Phenylalanine was detected in water samples collected from the Huron River, Michigan, collected at the Ann Arbor Water Treatment Plant in take line. Concentrations were 0.7 ng/L, not detected, and not detected on sampling dates 7/30/2003, 6/1/2004, and 6/29/2004, respectively(1).

NIOSH (NOES Survey 1981-1983) has statistically estimated that 19,901 workers (14,903 of these were female) were potentially exposed to (L)-phenylalanine in the US(1). Occupational exposure to (L)-phenylalanine may occur through inhalation and dermal contact with this compound at workplaces where (L)-phenylalanine is produced or used. Monitoring data indicate that the general population may be exposed to (L)-phenylalanine via ingestion of food or other consumer products containing (L)-phenylalanine(SRC).

Phenylalanine is an essential aromatic amino acid and is a precursor of melanin, dopamine, noradrenalin, and thyroxine(1).

L-phenylalanine may be helpful in some with depression. It may also be useful in the treatment of vitiligo. There is some evidence that L-phenylalanine may exacerbate tardive dyskinesia in some schizophrenic patients and in some who have used neuroleptic drugs.|Parenteral nutrition|Supplementation of amino-acids where parenteral nutrition is required.

An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.|/EXPTL TREATMENT/ There is no totally effective treatment for vitiligo (localised hypopigmentation). Oral or topical photochemotherapy with psoralens is generally considered to be the best available treatment, but experimental therapy includes UVA phototherapy with phenylalanine. Use of phenylalanine in oral doses of up to 100 mg/kg with UVA/sunlight led to beneficial results in more than 90% of 200 patients with vitiligo. Greatest benefit was noted in early disease, but prolonged use still induced repigmentation in long-standing cases. Repigmentation occurred mainly in areas rich in follicles. Such therapy is contra-indicated in phenylketonuria and in pregnancy. Similarly a further open study reported responses in 94 of 149 patients receiving 50 to 100 mg/kg daily of phenylalanine plus twice weekly UVA treatment. However, only 22% of responders had repigmentation in more than 60% of the affected area. Higher doses did not seem to be more effective than 50 mg/kg daily. Another group reported on 6 years of experience of treatment of vitiligo using 50 or 100 mg/kg daily of phenylalanine, with application of 10% phenylalanine gel and daily sun exposure. Although not ideal, they considered the treatment useful, especially for its ability to rapidly repigment the face. The same group performed an open study, adding topical 0.025% clobetasol propionate, and ultraviolet exposure during autumn and winter; 65.5% of patients achieved 100% repigmentation on the face.|/Experimental Therapy/ L-Phenylalanine (Phe), is a potent releaser of the satiety hormone, cholecystokinin (CCK) and previous studies, conducted primarily in men, show that ingestion of Phe reduces energy intake. The objective of the current study was to test the effects of Phe on energy intake in overweight and obese women. Subjects (n =3 2) received three treatments (high-dose (10 g Phe), low-dose (5 g Phe and 5 g glucose) or control (10 g glucose)) 20 min before an ad libitum lunch and dinner meal in a within-subjects', counterbalanced, double-blind study. No effect of Phe was found; however, interactions with dietary restraint status were detected in post-hoc analyses.|/Experimental Therapy/ L-phenylalanine in combination with 0.025% clobetasol propionate and sunlight during sunny months or UVA lamps in winter, appears to improve evolutive vitiligo without side effects, and therefore is especially recommended on the face or for children.|For more Therapeutic Uses (Complete) data for (L)-Phenylalanine (7 total), please visit the HSDB record page.

Overweight and obese women (n = 32) received three treatments (high-dose (10 g Phe), low-dose (5 g Phe and 5 g glucose) or control (10 g glucose)) 20 min before an ad libitum lunch and dinner meal. High-dose Phe increased ratings of nausea.

Used by the brain to produce Norepinephrine, a chemical that transmits signals between nerve cells and the brain; keeps you awake and alert; reduces hunger pains; functions as an antidepressant and helps improve memory.

Absorbed from the small intestine by a sodium dependent active transport process.|... It diffuses across placental membrane reaching higher fetal than maternal levels. In rhesus monkey when serum maternal levels are 1-2 mg/100 mL near full term there is an approx 1.5:1 diffusion rate, but when maternal levels ... high (25 mg/100 mL) fetal serum ... reach 45 mg/100 mL to detriment of fetus. /Phenylalanine/|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.|Table: Comparison of the Pool Sizes of Free and Protein-Bound Amino Acids in Rat Muscle [Table#3670]|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 bondspecific 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)-Phenylalanine (13 total), please visit the HSDB record page.

Hepatic. L-phenylalanine that is not metabolized in the liver is distributed via the systemic circulation to the various tissues of the body, where it undergoes metabolic reactions similar to those that take place in the liver.|Pathways of amino acid metabolism- L-phenylalanine; product of oxidative deamination or transamination: phenylpyruvic acid. Product of decarboxylation: phenylethylamine. Phenylalanine to tyrosine.|L-Phenylalanine yields in man: N-acetyl-L-phenylalanine; benzoic acid; probably in man, 2,5-dihydroxy-L-phenylalanine. /From table/|L-Phenylalanine yields in man: phenethylamine; phenylpyruvic acid; L-tyrosine. /From table/|L-Phenylalanine yields L-m-tyrosine in rat. /From table/|For more Metabolism/Metabolites (Complete) data for (L)-Phenylalanine (12 total), please visit the HSDB record page.

The supposed antidepressant effects of L-phenylalanine may be due to its role as a precursor in the synthesis of the neurotransmitters norepinephrine and dopamine. Elevated brain norepinephrine and dopamine levels are thought to be associated with antidepressant effects.
The mechanism of L-phenylalanine's possible antivitiligo activity is not well understood. It is thought that L-phenylalanine may stimulate the production of melanin in the affected skin|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. /Amino acids/

ACUTE/CHRONIC HAZARDS: When heated to decomposition this compound emits toxic fumes of nitrogen oxides. (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/ Adverse effects were not evident following acute single oral doses of L-phenylalanine as high as 10 g in 13 adult men.|/HUMAN EXPOSURE STUDIES/ Metabolic control in phenylketonuria (PKU) may be influenced by parental ability because dietary treatment involves complex food choices. This is an observational study to compare maternal carer (MC) knowledge and parental education with phenylalanine concentrations in children with PKU. Children (n = 46; 26 boys) aged 1-10 years (median age 6 years) on dietary treatment were recruited. Their median lifetime and median phenylalanine concentrations in the year prior to study were estimated. MC completed a questionnaire to assess dietary knowledge. Overall maternal knowledge on most aspects of diet was good and there was a correlation between annual median blood phenylalanine concentrations, but at the age of 5-6 years of age only, and higher maternal /caregiver/ scores on PKU knowledge (r = -0.646; p < 0.0001). Three of only four children (12%) with median phenylalanine concentrations above 500 umol/L in the year prior to study had both parents leave school without educational qualifications. Children who had median phenylalanine concentrations (n = 3; 7%) over the recommended ranges at 3 years of age or earlier continued to have poor control ...|/HUMAN EXPOSURE STUDIES/ The clinical severity of phenylalanine hydroxylase deficiency is usually defined by either pre-treatment phenylalanine (Phe) concentration or Phe tolerance at 5 years of age ... This study was conducted to investigate the course of the individual Phe tolerance and to assess the predictive value of both the pre-treatment Phe concentration and Phe tolerance at 1 and 6 months and 1, 2, 3, and 5 years for Phe tolerance at 10 years of age. Data on blood Phe concentration, prescribed Phe intake and weight of 213 early and continuously treated Dutch PKU patients up to 10 years of age were collected. Data acquired under good metabolic control were used in the study. Tolerance was expressed in mg/day and mg/kg per day. Data at 1 and 6 months and at 1, 2, 3, and 5 years of 61, 58, 59, 57, 56 and 59 patients were included for comparison with the Phe tolerance at 10 years. Phe tolerances (mg/kg per day) at 2, 3, and 5 years showed a clear correlation with the tolerance at 10 years of age (r = 0.608, r = 0.725 and r = 0.661). Results for tolerance expressed as mg/day were comparable. Pre-treatment Phe concentrations did not correlate significantly with the tolerance ...|/HUMAN EXPOSURE STUDIES/ The Maternal Phenylketonuria Study was designed to determine the effect of a phenylalanine (Phe)-restricted diet in reducing the morbidity on the fetus. Congenital abnormalities were noted, with the focus on the effect of congenital heart defects (CHDs) and microcephaly (MICRO) on developmental outcome at 4 and 6 years of age. Women with blood Phe levels > 240 umol/L (n=526; to convert umol/L to mg/dL, divide by 60) were enrolled; 382 contributed 572 pregnancies. The women had 413 offspring examined at birth and annually. At 4 years, the McCarthy General Cognitive Index was administered, and at 6 years, the Wechsler Intelligence Scale for Children Revised was administered. Microcephaly was noted in 137 (33%) of the offspring, and 32 (7.7%) had CHD. Maternal blood Phe levels were higher for infants with CHD and MICRO than for infants with CHD only (P=.02). Mean Phe levels at 4 to 8 weeks gestation predicted CHD (p <.0001). The McCarthy General Cognitive Index score was lower with CHD (p =.005) and MICRO (p =.0017), as was the Wechsler Intelligence Scale for Children Revised full-scale IQ score (p =.0002 for CHD and p =.0001 for MICRO). None of the subjects who had offspring with CHD had Phe control between 120 and 360 umol/L during the first 8 to 10 weeks of gestation ...|For more Human Toxicity Excerpts (Complete) data for (L)-Phenylalanine (26 total), please visit the HSDB record page.

Endorphenyl

Grades: Technical, FCC[Lewis RJ Sr; Hawley's Condensed Chemical Dictionary 15th ed Wiley (2007)|Available commercially as DL-dihydroxyphenylalanine and as DL-phenylalanine.[Lewis RJ Sr; Hawley's Condensed Chemical Dictionary 15th ed Wiley (2007)|Available commercially as the naturally occurring L(+)-enantiomer

All other basic organic chemical manufacturing|L-Phenylalanine: ACTIVE|Analysis of protein hydrolysates of bread indicated that ... phenylalanine ... degraded 5-17% during baking.|Amino acid composition of selected proteins- IUPAC abbreviation: PHE; gelatins 2.1 g/100 g; milk: mixed proteins 5.5 g/100 g; casein 5.0 g/100 g; serum albumin 7.0 g/100 g; gamma-globulin 4.6 g/100 g; hemoglobin: horse 7.7 g/100 g; insulin 8.1 g/100 g; clostridium botulinum toxin 1.2 g/100 g /Phenylalanine, from table/|Applications (Vet): in many protein hydrolysate mixtures for iv use (0.03-3.5 mg/mL in common commercial mixtures) ...|Precursor in biosynthetic pathway to epinephrine and norepinephrine|For more General Manufacturing Information (Complete) data for (L)-Phenylalanine (7 total), please visit the HSDB record page.

Method: AOAC 960.47; Procedure: microbiological, turbidimetric and titrimetric methods; Analyte: phenylalanine; Matrix: vitamin preparations; Detection Limit: not provided.|Method: AOAC 994.12; Procedure: performic acid oxidation with acid hydrolysis-sodium metabisulfite method; Analyte: phenylalanine; Matrix: feeds; Detection Limit: not provided.

BACKGROUND: Neonatal screening for congenital disorders like phenylketonuria (PKU), congenital hypothyroidism (CH), and congenital adrenal hyperplasia (CAH) is generally performed in dried blood spots on filter paper. The analytes of interest for testing for PKU, CH and CAH are phenylalanine, thyrotropin (TSH) and 17alpha-hydroxyprogesterone (17OHP), respectively. The International Society for Neonatal Screening (ISNS) /has prepared/ a combined reference preparation for the three analytes on filter paper Schleicher & Schuell #903, Whatman BFC180 and Toyo Roshi 545 ... The linearity of the blood spot calibrators and the homogeneity of the batch (only tested for Schleicher & Schuell) were good. The differences between the three filter papers were small /and it can be concluded that/ the 1st ISNS-RPNS for TSH, phenylalanine and 17OHP /is/ suitable as formal reference preparation and as a source for (re)calibrating kit calibrators.

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