Clinical Chemistry
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Clinical Chemistry 54: 1413-1414, 2008; 10.1373/clinchem.2008.110163
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(Clinical Chemistry. 2008;54:1413-1414.)
© 2008 American Association for Clinical Chemistry, Inc.


Editorials

CSF Serine Enantiomers and Glycine in the Study of Neurologic and Psychiatric Disorders

Kenji Hashimoto

Division of Clinical Neuroscience, Chiba University Center for Forensic Mental Health, Chiba, Japan

Address correspondence to the author at: Division of Clinical Neuroscience Chiba University Center for Forensic Mental Health 1-8-1 Inohana Chiba 260-8670, Japan Fax +81-423-226-2150 E-mail hashimoto@faculty.chiba-u.jp

The first 20% of the full text of this article appears below.

It was long believed that only the L-isomer of amino acids existed in mammals, and D–amino acids were regarded as laboratory artifacts and categorized as "unnatural" isomers. This term was widely used in textbooks of biochemistry. D–amino acids were known to be prominent in bacteria, and there were occasional reports of D–amino acids found in invertebrates (1). Hans Krebs accidentally discovered in kidney tissue an enzyme, D–amino acid oxidase (DAAO)1 , which recognized unnatural D–amino acids (but not their L-counterparts) (2). DAAO was found to degrade D–amino acids produced by bacteria from foods in the gut.

With the advance of chromatographic analysis techniques, small amounts of D–amino acids can now be measured in lower and higher animals, plants, and foods. By the use of 2-dimensional thin-layer chromatography and HPLC, Nagata et al. (3) found free D–amino acids, including D-serine, in kidney and blood of mutant mice lacking DAAO. Subsequently, Hashimoto and colleagues (4) demonstrated that D-serine was present in rat brain at high concentrations that were up to one-third those of L-serine, and that D-serine is heterogeneously distributed throughout rat brain with . . . [Full Text of this Article]







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