Enzymes in stereoselective pharmacokinetics of endogenous substances.
The use of enzymes to assay individual components of the L-carnitine family in pharmaceuticals, foodstuffs, and biological fluids with various forms of detection is reviewed. The most useful enzyme in the assay of compounds of the L-carnitine family is carnitine acetyl transferase (CAT), which catalyses the reversible interconversion of L-carnitine and its short-chain acyl esters. CAT can be used in one or more coupled reactions combined with U.V., or radiolabelled detection, or combined with HPLC, allowing, enantioselective, structurally specific, and, in the case of radiolabelled tracing, highly sensitive assays to be carried out. When compared with chromatographic separation of enantiomers or diastereoisomers, enantioselective enzyme mediated assays may be cheaper, more sensitive, and simpler, but they do not allow the nonpreferred isomer to be assayed. Consequently, they are appropriate for the specific assay of endogenous enantiomeric substrates of the enzyme concerned, in biological samples. The analysis of the other enantiomer in raw materials or in pharmaceuticals must be more properly approached by enantioselective chromatographic methods.
Marzo
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Department of Drug Metabolism and Pharmacokinetics, Sigma Tau S.p.A., Rome, Italy.
Cardace
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G
Arrigoni Martelli
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D002331:Carnitine / Q000032:analysis / Q000493:pharmacokinetics*; D004798:Enzymes; D006801:Humans; D013237:Stereoisomerism
D004798:Enzymes; D002331:Carnitine