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L0399905

Levocarnitine impurity A

European Pharmacopoeia (EP) Reference Standard

Synonym(s):

(E/Z)-4-(Trimethylammonio)but-2-enoate

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About This Item

Empirical Formula (Hill Notation):
C7H13NO2
CAS Number:
Molecular Weight:
143.18
UNSPSC Code:
41116107
NACRES:
NA.24

grade

pharmaceutical primary standard

API family

levocarnitine

manufacturer/tradename

EDQM

application(s)

pharmaceutical (small molecule)

format

neat

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

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.

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Eye Irrit. 2

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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K Eichler et al.
Molecular microbiology, 13(5), 775-786 (1994-09-01)
The sequence encompassing the cai genes of Escherichia coli, which encode the carnitine pathway, has been determined. Apart from the already identified caiB gene coding for the carnitine dehydratase, five additional open reading frames were identified. They belong to the
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
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
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

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