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12685

Sigma-Aldrich

Nω-Phospho-L-arginine lithium salt hydrate

≥95.0% (TLC)

Synonyme(s) :

H-Arg(PO3H2)-OH lithium salt, N5-(Phosphonoamidino)-L-ornithine lithium salt, N5-[Imino(phosphonoamino)methyl]-L-ornithine lithium salt, L-2-Amino-5-(N′-phosphonoguanidino)valeric acid lithium salt, Lithium L-arginine phosphate

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About This Item

Formule empirique (notation de Hill):
C6H15N4O5P · xLi+ · yH2O
Numéro CAS:
1189-11-3
Poids moléculaire :
254.18 (free acid basis)
Numéro CE :
214-714-7
Code UNSPSC :
12352209
Nomenclature NACRES :
NA.26

Pureté

≥95.0% (TLC)

Forme

powder or crystals

Couleur

white to off-white

Température de stockage

−20°C

InChI

1S/C6H15N4O5P/c7-4(5(11)12)2-1-3-9-6(8)10-16(13,14)15/h4H,1-3,7H2,(H,11,12)(H5,8,9,10,13,14,15)/t4-/m0/s1

Clé InChI

CCTIOCVIZPCTGO-BYPYZUCNSA-N

Actions biochimiques/physiologiques

Important metabolite in arginine and proline metabolism, high-energy metabolite, constituent of crustaceans and crayfish muscle.

Remarque sur l'analyse

may contain 8% more water then theoretically in monohydrate expected

Pictogrammes

Exclamation mark
GHS07

Mention d'avertissement

Warning

Mentions de danger

H315,H319,H335

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Gaspar E Canepa et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 160(1), 40-43 (2011-06-01)
Phytomonas are trypanosomatid plant parasites closely related to parasites that cause several human diseases. Little is known about the biology of these organisms including aspects of their metabolism. Arginine kinase (E.C. 2.7.3.3) is a phosphotransferase which catalyzes the interconversion between
Omar Davulcu et al.
Biochemistry, 50(19), 4011-4018 (2011-03-24)
Arginine kinase catalyzes the reversible transfer of a phosphoryl group between ATP and arginine. It is the arthropod homologue of creatine kinase, buffering cellular ATP levels. Crystal structures of arginine kinase, in substrate-free and substrate-bound forms, have revealed large conformational
Jonathan Bragg et al.
Journal of bacteriology, 194(10), 2668-2676 (2012-03-06)
Arginine kinases catalyze the reversible transfer of a high-energy phosphoryl group from ATP to l-arginine to form phosphoarginine, which is used as an energy buffer in insects, crustaceans, and some unicellular organisms. It plays an analogous role to that of
Margaret Werr et al.
Insect biochemistry and molecular biology, 39(9), 634-645 (2009-07-15)
Arginine kinase (ATP:l-arginine omega-N-phosphotransferase, EC2.7.3.3.; AK) is an enzyme crucial for the energy metabolism of insects and other invertebrates, that has known allergenic potential in humans and that has been proposed as a pesticidal drug target. Here we report the
Karina D García-Orozco et al.
International archives of allergy and immunology, 144(1), 23-28 (2007-05-15)
Consumption of seafood can produce allergic symptoms in susceptible individuals and crustacean allergies are the most frequently reported causes of allergic reactions. An allergen from the muscle of the white shrimp Litopenaeus vannamei was purified by ion exchange chromatography and

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