L-Arginine hydrochloride - CAS 1119-34-2

L-Arginine hydrochloride is the nitrogen donor for synthesis of nitric oxide, a potent vasodilator that is deficient during times of sickle cell crisis.
Protein supplement in health care products.

L-Amino Acids
Catalog number
CAS number
Molecular Formula
Molecular Weight
L-Arginine hydrochloride
(2S)-2-amino-5-(diaminomethylideneamino)pentanoic acid;hydrochloride
Arginine Hydrochloride; L-Arginine monohydrochloride; L-Arginine HCl; H-Arg-OH.HCl; (2S)-2-amino-5-(diaminomethylideneamino)pentanoic acid hydrochloride
Related CAS
74-79-3 (free acid)
White crystalline powder
1.42 g/cm3
Melting Point
Boiling Point
409.1ºC at 760 mmHg
Store at-20 °C
Soluble in Water
Ingredient of health care products.
InChI Key
Canonical SMILES
1.The effects of diet and arginine treatment on serum metabolites and selected hormones during the estrous cycle in sheep.
Kaminski SL1, Redmer DA1, Bass CS1, Keisler DH2, Carlson LS1, Vonnahme KA1, Dorsam ST1, Grazul-Bilska AT3. Theriogenology. 2015 Mar 15;83(5):808-16. doi: 10.1016/j.theriogenology.2014.11.017. Epub 2014 Nov 20.
The aim of this study was to determine the effects of diet and arginine (Arg) treatment on serum concentrations of selected metabolites and metabolic and reproductive hormones in nonpregnant ewes. Sixty days before the onset of estrus (Day 0), Rambouillet ewes were randomly assigned to one of three dietary groups: maintenance control (C; N = 16; 100% National Research Council requirements), overfed (O; N = 16; 2 × C), or underfed (U; N = 16, 0.6 × C) to achieve and maintain three different body conditions during their estrous cycle(s). At Day 0, ewes from each nutritional group were randomly assigned to receive one of two treatments: saline (Sal) or Arg (L-Arg-HCl; 155 μmol Arg per kg of body weight [BW]; intravenous), which was administered three times per day for 21 or 26 days. Blood samples were collected on Days 0, 6, 10, 12, 16, 21, and 26 of Sal or Arg treatment for evaluation of Arg, nitric oxide metabolite, cholesterol, glucose, insulin, insulin-like growth factor 1, leptin, and progesterone.
2.Photocytotoxicity and DNA cleavage activity of L-arg and L-lys Schiff base oxovanadium(IV) complexes having phenanthroline bases.
Sasmal PK1, Majumdar R, Dighe RR, Chakravarty AR. Dalton Trans. 2010 Aug 14;39(30):7104-13. doi: 10.1039/c001867h. Epub 2010 Jun 19.
Oxovanadium(IV) complexes [VO(sal-argH)(B)]Cl (1-3) and [VO(sal-lysH)(B)]Cl (4-6), where sal-argH2 and sal-lysH2 are N-salicylidene-L-arginine and N-salicylidene-L-lysine Schiff bases and B is a phenanthroline base, viz. 1,10-phenanthroline (phen in 1 and 4); dipyrido[3,2-d:2',3'-f]quinoxaline (dpq in 2 and 5) and dipyrido[3,2-a:2',3'-c]phenazine (dppz in 3 and 6), have been prepared, characterized and their DNA photocleavage activity studied. Complex 1, characterized by X-ray crystallography, shows the presence of a vanadyl group in V(IV)O3N3 coordination geometry with a tridentate Schiff base having a pendant guanidinium moiety and bidentate phen ligand. The complexes exhibit a d-d band at 715 nm in 20% DMF-Tris-HCl buffer. The complexes are redox active showing cathodic and anodic responses near -1.0 V and 0.85 V (vs. SCE) for the V(IV)-V(III) and V(V)-V(IV) couples, respectively, in DMF-Tris-HCl buffer. The complexes bind to calf thymus DNA giving Kb values in the range of 3.
3.Copper(II) complexes of L-arginine as netropsin mimics showing DNA cleavage activity in red light.
Patra AK1, Bhowmick T, Roy S, Ramakumar S, Chakravarty AR. Inorg Chem. 2009 Apr 6;48(7):2932-43. doi: 10.1021/ic8017425.
Copper(II) complexes [Cu(L-arg)(2)](NO(3))(2) (1) and [Cu(L-arg)(B)Cl]Cl (2-5), where B is a heterocyclic base, namely, 2,2'-bipyridine (bpy, 2), 1,10-phenanthroline (phen, 3), dipyrido[3,2-d:2',3'-f]quinoxaline (dpq, 4), and dipyrido[3,2-a:2',3'-c]phenazine (dppz, 5), are prepared and their DNA binding and photoinduced DNA cleavage activity studied. Ternary complex 3, structurally characterized using X-ray crystallography, shows a square-pyramidal (4 + 1) coordination geometry in which the N,O-donor L-arginine and N,N-donor 1,10-phenanthroline form the basal plane with one chloride at the elongated axial site. The complex has a pendant cationic guanidinium moiety. The one-electron paramagnetic complexes display a metal-centered d-d band in the range of 590-690 nm in aqueous DMF. They show quasireversible cyclic voltammetric response due to the Cu(II)/Cu(I) couple in the range of -0.1 to -0.3 V versus a saturated calomel electrode in a DMF-Tris HCl buffer (pH 7.
4.π-Cation interactions as the origin of the weak absorption at 532 nm observed in tryptophan-containing polypeptides.
Roveri OA1, Braslavsky SE. Photochem Photobiol Sci. 2012 Jun;11(6):962-6. doi: 10.1039/c2pp05341a. Epub 2012 Jan 25.
We have previously reported that bovine serum albumin (BSA) and other proteins that do not contain prosthetic groups exhibited a weak light absorption in the visible, only detectable by pulsed laser-induced optoacoustic spectroscopy (LIOAS). Human serum albumin (HSA) exhibited signals 25% higher than those observed with BSA. Signals comparable to those obtained with BSA were observed with poly(L-Trp, L-Lys), poly(L-Trp, L-Arg) or poly(L-Trp, L-Orn) at pH 7.0. No signals were obtained when tryptophan was replaced by other amino acids or when free tryptophan or the tripeptide Lys-Trp-Lys was assayed (pH 7.0). Tryptophan in HCl 5 N produced LIOAS signals similar to those produced by tryptophan-containing copolymers. Moreover, the absorption peak could be observed in a UV-VIS spectrophotometer. Therefore, the LIOAS signals obtained with BSA, HSA, and tryptophan-containing random copolymers may be attributed to a new transition of the indole moiety of their tryptophan residues when "protonated".
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