Determination of d- and l-enantiomers of methionine and [2H3]methionine in plasma by gas chromatography–mass spectrometry

Hasegawa, Hiroshi; Shinohara, Yoshihiko; Akahane, Kenji; Hashimoto, Takao

doi:10.1016/j.jchromb.2005.06.010

Cited by 6 publications

(6 citation statements)

References 21 publications

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“…L-Methionine appeared rapidly after administration of D-methionine, with the inversion fraction of more than 90%. The result demonstrated that almost all intravenous administered D-methionine is thus converted into the L-enantiomer in vivo [36,37].…”

Section: D-methioninementioning

confidence: 91%

“…This is possible because D-NNA and L-NNA are unique exogenous substances and endogenous interference is absent. This is in contrast to naturally occurring compounds such as D-leucine [33][34][35] and D-methionine [36][37][38]. These latter formed L-amino acids and -keto acids are indistinguishable from endogenous ones, and would therefore require complicated combined methods of isotope labeling utility and gas chromatography-mass (GC-MS) to monitor in vivo chiral inversion [33][34][35][36][37][38] (see below).…”

Section: Nnamentioning

confidence: 99%

“…Because of potential radiation hazard to humans, the stable isotope method is more desirable than the radiotracer technique for providing useful pharmacokinetic data. Hasegawa's group successfully combined the indirect chiral separation and stable isotope technologies to separate endogenous and exogenous D-and L-enantiomers of leucine and methionine [33][34][35][36][37][38].…”

Section: D-leucinementioning

confidence: 99%

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Biological Implications of Oxidation and Unidirectional Chiral Inversion of D-amino Acids

Wang¹,

Gong²,

Xin³

et al. 2012

CDM

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Recent progress in chiral separation of D- and L-amino acids by chromatography ascertained the presence of several free Damino acids in a variety of mammals including humans. Unidirectional chiral inversion of many D-amino acid analogs such as exogenous NG-nitro-D-arginine (D-NNA), endogenous D-leucine, D-phenylanine and D-methionine have been shown to take place with inversion rates of 4-90%, probably dependent on various species D-amino acid oxidase (DAAO) enzymatic activities. DAAO is known to catalyze the oxidative deamination of neutral and basic D-amino acids to their corresponding α-keto acids, hydrogen peroxide and ammonia, and is responsible for the chiral inversion. This review provides an overview of recent research in this area: 1) oxidation and chiral inversion of several D-amino acid analogs in the body; 2) the indispensable but insufficient role of DAAO particularly in the kidneys and brain for the oxidation and chiral inversion of D-amino acids analogs; and 3) unidentified transaminase(s) responsible for the second step of chiral inversion. The review also discusses the physiological significance of oxidation and chiral inversion of D-amino acids, which is still a subject of dispute.

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Section: D-methioninementioning

confidence: 91%

Section: Nnamentioning

confidence: 99%

Section: D-leucinementioning

confidence: 99%

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Biological Implications of Oxidation and Unidirectional Chiral Inversion of D-amino Acids

Wang¹,

Gong²,

Xin³

et al. 2012

CDM

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“…() performed stereoselective determination of the endogenous and labeled d ‐ and l ‐enantiomers of methionine and [ 2 H 3 ] methionine in rat plasma with the use of GC‐MS‐SIM. The amino acids were derivatized to methyl esters and then N ‐acetylated with the use of optically active (+)‐ α ‐methoxy‐ α ‐trifluoromethylphenylacetyl chloride to form diastereoisomeric amides (Hasegawa et al ., ). Separation of those amino acid enantiomers was performed on a methylsilicone‐bonded phase fused‐silica capillary column SPB‐1 (15 m × 0.25 mm).…”

Section: Gas Chromatography In Amino Acid and Peptide Separationmentioning

confidence: 99%

Application of TLC, HPLC and GC methods to the study of amino acid and peptide enantiomers: a review

Dołowy

Pyka

2013

Biomedical Chromatography

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Amino acids are very important organic compounds in nature. The biological activity of amino acids depends mainly on their stereoisomeric configuration (d- or l-). Thus, the stereochemical analysis of amino acids and peptides is an important aspect of their characterization. Owing to the increasing role of amino acid configuration in biomedical and pharmaceutical studies, numerous analytical methods have been described in the literature. Among a wide range of analytical techniques available for the steroselective separation of different amino acids, which were obtained from plants or biological samples, chromatographic methods such as thin-layer chromatography, high-performance chromatography and also gas chromatography are very useful. This review presents such systems developed for direct stereoisomeric separation and quantitative determination of amino acid and peptide enantiomers with emphasis on selected literature published during two last decades. Almost all aspects, including sample preparation prior chromatographic analysis, stationary phase, solvent system and detection system, are discussed. New possibilities in chiral amino acid analysis have been opened up by the application of mass spectrometry and infrared detection in thin-layer chromatography and mass spectrometry-selected ion monitoring detection system in gas chromatography. A modern trend in high-performance chromatography is two-dimensional chromatography. These innovations have led to decreased development time and increased amino acid resolution and detectability.

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“…In our previous study, the use of stable isotope labeled D-methionine and the stereoselective gas chromatographymass spectrometry-selected ion monitoring (GC-MS-SIM) method 7) proved to be a powerful methodology for examining the pharmacokinetic behavior of exogenously administered D-methionine and for studying the conversion of D-methionine into the L-enantiomer. We have shown that almost all Dmethionine exogenously administered were converted into the L-enantiomer in rats.…”

mentioning

confidence: 99%

Synthesis of D- and L-Selenomethionine Double-Labeled with Deuterium and Selenium-82

Matsukawa

Hasegawa

Shinohara

et al. 2010

CHEMICAL & PHARMACEUTICAL BULLETIN

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Selenium has been recognized as an essential element of human nutrition. Various forms of selenium, such as selenite, selenate, selenocysteine and selenomethionine, can be utilized as nutritional sources. [1][2][3][4] Since selenomethionine is more effective and less toxic than inorganic selenium, synthetic selenomethionine or its enriched food sources are appropriate supplemental forms of selenium. David et al. 5) reported that some formula contained racemic selenomethionine. McAdam and Levander 6) showed little difference in the acute toxicity and nutritional bioavailability between D-and L-selenomethionine in rats and suggested that D-selenomethionine might be converted into the L-enantiomer. L-Selenomethionine is transformed to L-selenohomocysteine, similarly to the de-methylation pathway for L-methionine to Lhomocysteine. Then, L-selenohomocysteine is re-methylated to reform L-selenomethionine, or condensed with L-serine to form L-selenocystathionine, which is transformed to L-selenocysteine. However, little information is available on the metabolic fate of D-selenomethionine, especially conversion of D-selenomethionine into the L-enantiomer.In our previous study, the use of stable isotope labeled D-methionine and the stereoselective gas chromatographymass spectrometry-selected ion monitoring (GC-MS-SIM) method 7) proved to be a powerful methodology for examining the pharmacokinetic behavior of exogenously administered D-methionine and for studying the conversion of D-methionine into the L-enantiomer. We have shown that almost all Dmethionine exogenously administered were converted into the L-enantiomer in rats. 8)We have initiated studies to characterize the pharmacokinetic behavior of selenomethionine enantiomers by the stable isotope methodology. Successful application of the methodology to the metabolic investigation is dependent upon the availability of compounds labeled at predesigned positions. The present paper describes the preparation of optically pure D-and L-selenomethionine double-labeled with three deuteriums and 82 Se. Results and DiscussionConvenient synthetic routes to selenomethionine labeled on selenium 9-11) or methyl group 12) have been published, but the synthesis of deuterium and 82 Se double-labeled selenomethionine has not been reported. With few exceptions, the synthesis of Se-labeled selenomethionine had been achieved by treating 2-amino-4-bromobutanoic acid with a labeled lithium methaneselenolate.The synthetic route to D-and L-[ 2 H 3 , 82 Se]selenomethionine is illustrated in Chart 1. 2-Amino-4-bromobutanoic acid, a key intermediate in this synthesis, was obtained by either ring opening of 2-amino-4-butyrolactone (homoserine lactone) with HBr 13) or bromination of 2-amino-4-hydroxybutanoic acid (homoserine) with HBr in AcOH. 14) We have synthesized (R)-2-amino-4-hydroxybutanoic acid (2a) from commercially available D-homoserine lactone (1a) yielding Pharmacy and Life Sciences; 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan: and c Research Institute for Cultural Sc...

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Determination of d- and l-enantiomers of methionine and [2H3]methionine in plasma by gas chromatography–mass spectrometry

Cited by 6 publications

References 21 publications

Biological Implications of Oxidation and Unidirectional Chiral Inversion of D-amino Acids

Biological Implications of Oxidation and Unidirectional Chiral Inversion of D-amino Acids

Application of TLC, HPLC and GC methods to the study of amino acid and peptide enantiomers: a review

Synthesis of D- and L-Selenomethionine Double-Labeled with Deuterium and Selenium-82

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