74-79-3 Usage
Description
L(+)-Arginine, also known as L-arginine, is an essential amino acid that plays a crucial role in various biological processes, including the synthesis of proteins, the urea cycle, and the production of nitric oxide. It is characterized by its guanidino group and is predominantly found in the L-configuration.
Uses
Used in Cardiovascular Health:
L(+)-Arginine is used as a therapeutic agent for heart and blood vessel conditions such as congestive heart failure (CHF), chest pain, high blood pressure, and coronary artery disease. Its antiatherogenic, anti-ischemic, antiplatelet, and antithrombotic properties make it vital in the treatment of cardiovascular diseases.
Used in Erectile Dysfunction Treatment:
L(+)-Arginine is used as a growth stimulant in the treatment of erectile dysfunction in men, helping to improve blood flow and enhance sexual performance.
Used in Dental Care:
L(+)-Arginine is used as an active ingredient in toothpaste, providing effective relief for sensitive teeth and promoting overall oral health.
Used in Cell Culture Media:
L(+)-Arginine is used as a component of Roswell Park Memorial Institute (RPMI) media for the isolation and culture of peripheral blood mononuclear cells (PBMCs) and tissue culture applications. It is also used in Dulbecco's Modified Eagle Medium (DMEM) for the identification and quantification of phosphorylation sites by stable isotope labeling by amino acids in cell culture (SILAC) and liquid chromatography-tandem mass spectrometry (LCMS/MS) analysis.
Used as a Nutrient:
L(+)-Arginine is used as an essential amino acid and nutrient, playing a critical role in the synthesis of proteins and various metabolic pathways in the human body.
Indications and Usage
Odorless, slightly bitter. Easily soluble in water (solubility in 0℃ water is 83g/L, solubility in 50℃ water is 400g/L), very slightly soluble in ethanol, insoluble in ether; pI6.0; loses its 2-molecule water crystal when heated to 105℃, darkens in color at 230℃, disintegrates at 244℃; its aqueous solution has maximum absorption at 205nm (1gε3.28).
L-Arginine is an encoding amino acid in protein synthesis and is one of the 8 essential amino acids in the human body. The body needs it for many different functions. Taking L-Arginine supplements can treat certain diseases such as congestive heart failure and cystitis. L-Arginine can also act as seasoning for nutrient supplements and food additives. L-Arginine can undergo a heat reaction with sugar (amino-carbonyl reaction) to obtain a unique fragrance, GB 2760-2001, an approved food spice. As an amino acid drug, L-Arginine can be used as pharmaceutical raw material and is an important ingredient in amino acid infusions and integrated amino acid preparations. It is also a crucial amino acid in maintaining infant growth and maturation.
Mechanisms of Action
L-Arginine can stimulate the human body to release certain chemicals such as insulin and human growth hormone. It can also clear ammonia in the body and promote the healing of wounds. The human body also needs it to produce sarcosine. Decomposing L-Arginine produces nitric oxide, which can expand blood vessels and increase blood flow. L-Arginine is an intermediate metabolite in the orthinine cycle and promotes the conversion of ammonia to urea, thus lowering the blood concentration of ammonia. L-Arginine is also an important part of sperm protein and can promote spermatogenesis and provide energy for sperm movement. Additionally, intravenous arginine can stimulate the pituitary to release growth hormone and can be used to test pituitary functions.
Adverse reactions
Abdominal pain, diarrhea, gout and bloating. There may also be increased severity in herpes breakouts and increased effects of antihypertensive drugs, resulting in a lower blood pressure than expected, which may cause hypertensive patients to experience dizziness and fainting.
Toxicity Level
Moderate
Acute Toxicity
Reference data: abdominal cavity – large rat LD50: 3793 mg/kg.
Flammability Characteristics
Flammable. Burning produces toxic nitrogen oxide smoke.
Handling
Store in ventilated, cool and dry area.
Extinguishers
Dry powder, foam, sand, carbon dioxide, water mist.
Biochem/physiol Actions
Substrate of nitric oxide synthase, which is converted to citrulline and nitric oxide (NO). Induces insulin release by a nitric oxide-dependent mechanism.
Safety Profile
Mutation data reported. Whenheated to decomposition it emits toxic fumes of NOx.
Synthesis
Enzymatically, arginine is formed in two reactions from citrulline. The first reaction (citrulline + succinate) is catalyzed
by the enzyme arginosuccinate synthetase. It is ATP dependent and with the formation of a new C–N bond in the gaunidino group of
arginosuccinate, water is removed and ATP is hydrolyzed. The second reaction is catalyzed by arginine synthetase and involves the
scission of arginosuccinate with the formation of arginine and fumaric acid.
Purification Methods
S-Arginine crystallises from H2O as the dihydrate and as plates from EtOH. It also crystallises from 66% EtOH. Its solubility in H2O is 15% at 21o. Its isoelectric point is at pH 10.76. [Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 p 1841 1961, Beilstein 4 IV 817.]
Check Digit Verification of cas no
The CAS Registry Mumber 74-79-3 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 7 and 4 respectively; the second part has 2 digits, 7 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 74-79:
(4*7)+(3*4)+(2*7)+(1*9)=63
63 % 10 = 3
So 74-79-3 is a valid CAS Registry Number.
InChI:InChI=1/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/p+1/t4-/m0/s1
74-79-3Relevant articles and documents
Direct monitoring of biocatalytic deacetylation of amino acid substrates by1H NMR reveals fine details of substrate specificity
De Cesare, Silvia,McKenna, Catherine A.,Mulholland, Nicholas,Murray, Lorna,Bella, Juraj,Campopiano, Dominic J.
supporting information, p. 4904 - 4909 (2021/06/16)
Amino acids are key synthetic building blocks that can be prepared in an enantiopure form by biocatalytic methods. We show that thel-selective ornithine deacetylase ArgE catalyses hydrolysis of a wide-range ofN-acyl-amino acid substrates. This activity was revealed by1H NMR spectroscopy that monitored the appearance of the well resolved signal of the acetate product. Furthermore, the assay was used to probe the subtle structural selectivity of the biocatalyst using a substrate that could adopt different rotameric conformations.
Argicyclamides A-C Unveil Enzymatic Basis for Guanidine Bis-prenylation
Balloo, Nandani,Fujita, Kei,Matsuda, Kenichi,Okino, Tatsufumi,Phan, Chin-Soon,Wakimoto, Toshiyuki
supporting information, p. 10083 - 10087 (2021/07/26)
Guanidine prenylation is an outstanding modification in alkaloid and peptide biosynthesis, but its enzymatic basis has remained elusive. We report the isolation of argicyclamides, a new class of cyanobactins with unique mono- and bis-prenylations on guanidine moieties, from Microcystis aeruginosa NIES-88. The genetic basis of argicyclamide biosynthesis was established by the heterologous expression and in vitro characterization of biosynthetic enzymes including AgcF, a new guanidine prenyltransferase. This study provides important insight into the biosynthesis of prenylated guanidines and offers a new toolkit for peptide modification.
Development of a Raltegravir-based Photoaffinity-Labeled Probe for Human Immunodeficiency Virus-1 Integrase Capture
Pala, Nicolino,Esposito, Francesca,Tramontano, Enzo,Singh, Pankaj Kumar,Sanna, Vanna,Carcelli, Mauro,Haigh, Lisa D.,Satta, Sandro,Sechi, Mario
supporting information, p. 1986 - 1992 (2020/11/09)
Photoaffinity labeling (PAL) is one of the upcoming and powerful tools in the field of molecular recognition. It includes the determination of dynamic parameters, such as the identification and localization of the target protein and the site of drug binding. In this study, a photoaffinity-labeled probe for full-length human immunodeficiency virus-1 integrase (HIV-1 IN) capture was designed and synthesized, following the structure of the FDA-approved drug Raltegravir. This photoprobe was found to retain the HIV IN inhibitory potential in comparison with its parent molecule and demonstrates the ability to label the HIV-1 IN protein. Putative photoprobe/inhibitor binding sites near the catalytic site were then identified after protein digestion coupled to mass and molecular modeling analyses.