Cholinesterase-catalyzed resolution of D,L-carnitine.
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.
Dropsy
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Laboratory of Applied Biochemistry, Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
Klibanov
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