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Dropsy EP, Klibanov AM. Cholinesterase-catalyzed resolution of D,L-carnitine. Biotechnol Bioeng. 1984;26(8):911-5doi: 10.1002/bit.260260815.
Dropsy, E. P., & Klibanov, A. M. (1984). Cholinesterase-catalyzed resolution of D,L-carnitine. Biotechnology and bioengineering, 26(8), 911-5. https://doi.org/10.1002/bit.260260815
Dropsy, E P, and Klibanov, A M. "Cholinesterase-catalyzed resolution of D,L-carnitine." Biotechnology and bioengineering vol. 26,8 (1984): 911-5. doi: https://doi.org/10.1002/bit.260260815
Dropsy EP, Klibanov AM. Cholinesterase-catalyzed resolution of D,L-carnitine. Biotechnol Bioeng. 1984 Aug;26(8):911-5. doi: 10.1002/bit.260260815. PMID: 18553477.
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Biotechnol Bioeng. 1984 Aug;26(8):911-5. doi: 10.1002/bit.260260815.

Cholinesterase-catalyzed resolution of D,L-carnitine.

Biotechnology and bioengineering

E P Dropsy, A M Klibanov

Affiliations

  1. Laboratory of Applied Biochemistry, Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.

PMID: 18553477 DOI: 10.1002/bit.260260815

Abstract

An enzymatic method for the preparative resolution of racemic carnitine (whose L-isomer and its acyl-derivatives have numerous therapeutical applications) has been developed. It is based on our finding that electriceel acetylcholinesterase hydrolyzes the D- but not the L-isomer of acetylcarnitine. (Another cholinesterase tested, horse serum butyrylcholinesterase, is also stereospecific and hydrolyzes only the L-isomer of butyrylcarnitine.) Acetylcholinesterase, covalently attached to alumina, was employed for the resolution of D,L-carnitine; the latter was first chemically acetylated, then stereoselectively hydrolyzed with the immobilized enzyme, and finally the acetyl-L-carnitine and D-carnitine produced were separated by ion-exchange chromatography. Gram quantities of D,L-carnitine were thereby resolved.

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