SMILES string
[N+](C\C=C\C(=O)[O-])(C)(C)C
InChI
1S/C7H13NO2/c1-8(2,3)6-4-5-7(9)10/h4-5H,6H2,1-3H3/b5-4+
InChI key
GUYHPGUANSLONG-SNAWJCMRSA-N
grade
pharmaceutical primary standard
API family
levocarnitine
manufacturer/tradename
EDQM
application(s)
pharmaceutical (small molecule)
format
neat
General description
This product is provided as delivered and specified by the issuing Pharmacopoeia. All information provided in support of this product, including SDS and any product information leaflets have been developed and issued under the Authority of the Issuing Pharmacopoeia. For further information and support please go to the website of the issuing Pharmacopoeia.
Application
Levocarnitine impurity A EP Reference standard, intended for use in laboratory tests only as specifically prescribed in the European Pharmacopoeia.
Packaging
The product is delivered as supplied by the issuing Pharmacopoeia. For the current unit quantity, please visit the EDQM reference substance catalogue.
Other Notes
Sales restrictions may apply.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
J M Obón et al.
Applied microbiology and biotechnology, 51(6), 760-764 (1999-07-28)
The use of a biological procedure for L-carnitine production as an alternative to chemical methods must be accompanied by an efficient and highly productive reaction system. Continuous L-carnitine production from crotonobetaine was studied in a cell-recycle reactor with Escherichia coli
M R Castellar et al.
Journal of applied microbiology, 85(5), 883-890 (1998-11-27)
L(-)-carnitine was produced from D(+)-carnitine by resting cells of Escherichia coli O44 K74. Oxygen did not inhibit either the carnitine transport system or the enzymes involved in the biotransformation process. Aerobic conditions led to higher product yield than anaerobic conditions.
Manuel Cánovas et al.
Journal of basic microbiology, 43(4), 259-268 (2003-07-23)
The biotransformation of crotonobetaine and D(+)-carnitine into L(-)-carnitine is affected by salt stress in the resting cells of E. coli O44 K74 and the transformed E. coli K38 pT7-5KE32. A yield of 65 and 80% of L(-)-carnitine, respectively, were obtained
C Engemann et al.
Archives of microbiology, 175(5), 353-359 (2001-06-21)
Two proteins, component I (CI) and component II (CII), catalyze the biotransformation of crotonobetaine to L(-)-carnitine in Proteus sp. CI was purified to electrophoretic homogeneity from cell-free extracts of Proteus sp. The N-terminal amino acid sequence of CI showed high
T Elssner et al.
Biochemistry, 39(35), 10761-10769 (2000-09-09)
A still unknown low-molecular-mass cofactor essential for the activity of carnitine-metabolizing enzymes (e.g., L-carnitine dehydratase, crotonobetaine reductase) from E. coli has been purified to homogeneity from a cell-free extract of E. coli O44K74. The purity of the cofactor was confirmed
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