Not available outside of the UK & Ireland.

Application

Determination of L-carnitine in seminal plasma, serum, or urine in life science research applications.

Biochem/physiol Actions

L-carnitine is an abundant amino acid present in red meat. Its trimethylamine structure has similarity to that of choline. The major source of this amino acid is by dietary ingestion. In mammals, it is also endogenously produced from lysine. It participates in the transport of fatty acids into the mitochondrial compartment. It produces trimethylamine-N-oxide (TMAO) and promotes atherosclerosis.

General description

Enzymatic UV-Test with a linearity in the range of 5.6 - 112 µM L-carnitine in the test solution.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Packaging

1 kit containing 6 components

Preparation Note

Storage conditions (working solution): Note: After reconstitution, the solution 1 is stable for 4 days at 2 to 8 °C. Bring solution 1 to 15 to 25 °C prior to use. After reconstitution, the suspension 2 is stable for 3 months at 2 to 8 °C.

Principle

L-Carnitine is acetylated to acetyl carnitine by acetyl coenzyme A (acetyl CoA) in the presence of the enzyme carnitine acetyl transferase (CAT). The resulting coenzyme A (CoA) is acetylated back to acetyl CoA in the presence of adenosine-5’-triphosphate (ATP) and acetate, catalyzed by the enzyme acetyl CoA synthetase (ACS). This results in the formation of adenosine-5’-monophosphate (AMP) and inorganic pyrophosphate (PPi). In the presence of ATP, supported by myokinase (MK), AMP forms twice the amount of adenosine-5’-diphosphate (ADP). This is converted in the following reaction with phosphoenol pyruvate (PEP) in the presence of pyruvate kinase (PK). The pyruvate formed is reduced to L-lactate by reduced nicotinamide adenine dinucleotide (NADH) in the presence of lactate dehydrogenase (LDH). The amount of NADH consumed during the reaction is equivalent to half the amount of L-carnitine. NADH is measured spectroscopically at 340 nm.