Comparison of derivatization and chromatographic methods for GC–MS analysis of amino acid enantiomers in physiological samples

Waldhier, Magdalena C.; Dettmer, Katja; Gruber, Michael; Oefner, Peter J.

doi:10.1016/j.jchromb.2010.03.021

Cited by 53 publications

(29 citation statements)

References 26 publications

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“…GC/MS method employing RT-γDEXsa (2,3-di-acetoxy-6-O-tert-butyl-dimethylsilyl γ-CD doped into 14% cyanopropylphenyl/86% dimethyl polysiloxane) column for AA determination in human serum and urine was developed and applied to urine samples from patients with renal insufficiency [95]. The method required protein removal by precipitation before AA derivatization with methyl chloroformate/methanol and reaction performance at neutral pH.…”

Section: Chromatographic Determination Of Aas As Possible Biomarkers mentioning

confidence: 99%

Enantiomeric Ratio of Amino Acids as a Tool for Determination of Aging and Disease Diagnostics by Chromatographic Measurement

2016

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Abstract:Occurrence of D-amino acids in living organisms is a useful indicator of various changes, diseases, or disorders. Determination of amino acid enantiomers, namely the enantiomeric ratio of amino acids or excess of certain D-amino acids, represents a useful tool in the studies of aging processes or biomarkers in disease/disorder diagnosis in humans. The amount of D-amino acids is usually very low. Therefore, suitable sample pretreatment, often derivatization, and highly selective and sensitive separation methods are essential for D-amino acid analysis in this field. Chromatographic techniques offer appropriate choices for solving these tasks. This review covers the advances in methodology and development of improved instrumental chromatographic methods focused on D,L-amino acid separation and determination. New findings in the area of possible D-amino acid biomarkers are also included.

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Section: Chromatographic Determination Of Aas As Possible Biomarkers mentioning

confidence: 99%

Enantiomeric Ratio of Amino Acids as a Tool for Determination of Aging and Disease Diagnostics by Chromatographic Measurement

2016

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“…Individual amino acids were identified and quantified by gas chromatography (GC) and GC mass spectrometry (GC/MS) using the EZFaast method (Phenomenex, Torrance, CA, USA), which uses derivatization of AAs with propyl chloroformate and propanol for sensitive detection (see [46] for a comparison of the methods). Briefly, sediment samples, sediment buffer mixtures, T. weissflogii buffer mixtures and gel section electroelutions were hydrolyzed for 4 h at 110 °C [47,48] with 6 M analytical-grade HCl and L-methylleucine as the recovery standard.…”

Section: Total Hydrolysable Amino Acid Analysismentioning

confidence: 99%

Electrophoretic Extraction and Proteomic Characterization of Proteins Buried in Marine Sediments

et al. 2014

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Abstract:Proteins are the largest defined molecular component of marine organic nitrogen, and hydrolysable amino acids, the building blocks of proteins, are important components of particulate nitrogen in marine sediments. In oceanic systems, the largest contributors are phytoplankton proteins, which have been tracked from newly produced bloom material through the water column to surface sediments in the Bering Sea, but it is not known if proteins buried deeper in sediment systems can be identified with confidence. Electrophoretic gel protein extraction methods followed by proteomic mass spectrometry and database searching were used as the methodology to identify buried phytoplankton proteins in sediments from the 8-10 cm section of a Bering Sea sediment core. More peptides and proteins were identified using an SDS-PAGE tube gel than a standard 1D flat gel or digesting the sediment directly with trypsin. The majority of proteins identified correlated to the marine diatom, Thalassiosira pseudonana, rather than bacterial protein sequences, indicating an algal source not only dominates the input, but also the preserved protein fraction. Abundant RuBisCO and fucoxanthin chlorophyll a/c binding proteins were identified, supporting algal sources of these proteins and reinforcing the proposed mechanisms that might protect proteins for long time periods. Some preserved peptides were identified in OPEN ACCESSChromatography 2014, 1 177 unexpected gel molecular weight ranges, indicating that some structural changes or charge alteration influenced the mobility of these products during electrophoresis isolation. Identifying buried photosystem proteins suggests that algal particulate matter is a significant fraction of the preserved organic carbon and nitrogen pools in marine sediments.

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“…Newer analytical techniques have allowed the determination of trace levels of D-Thr in other physiologic tissues amidst excessive L-isomers (Hamase et al 2009;Waldhier et al 2010). The four isomers of Thr were resolved using a two-dimensional HPLC system and measured in various tissue of mammals (Hamase 2007;Zhao et al 2004).…”

Section: D-serinementioning

confidence: 99%

“…L-Allo-Thr was not detected, suggesting that the epimerization of the chiral center of the a-carbon predominantly occurs, compared with the epimerization of the b-carbon (Zhao et al 2004). Another technique of derivatization combined with GC/MS allowed simultaneous determination of L-and D-Thr in a single run (Waldhier et al 2010). They were able to determine with this technique that patients suffering from renal failure were found to have significantly higher ratios of D-Thr to L-Thr than healthy controls (Waldhier et al 2010).…”

Section: D-serinementioning

confidence: 99%

“…Another technique of derivatization combined with GC/MS allowed simultaneous determination of L-and D-Thr in a single run (Waldhier et al 2010). They were able to determine with this technique that patients suffering from renal failure were found to have significantly higher ratios of D-Thr to L-Thr than healthy controls (Waldhier et al 2010). …”

Section: D-serinementioning

confidence: 99%

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Nutritional and medicinal aspects of d-amino acids

2011

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This paper reviews and interprets a method for determining the nutritional value of D-amino acids, D-peptides, and amino acid derivatives using a growth assay in mice fed a synthetic all-amino acid diet. A large number of experiments were carried out in which a molar equivalent of the test compound replaced a nutritionally essential amino acid such as L-lysine (L-Lys), L-methionine (L-Met), L-phenylalanine (L-Phe), and L-tryptophan (L-Trp) as well as the semi-essential amino acids L-cysteine (L-Cys) and L-tyrosine (L-Tyr). The results show wide-ranging variations in the biological utilization of test substances. The method is generally applicable to the determination of the biological utilization and safety of any amino acid derivative as a potential nutritional source of the corresponding L-amino acid. Because the organism is forced to use the D-amino acid or amino acid derivative as the sole source of the essential or semi-essential amino acid being replaced, and because a free amino acid diet allows better control of composition, the use of all-amino-acid diets for such determinations may be preferable to protein-based diets. Also covered are brief summaries of the widely scattered literature on dietary and pharmacological aspects of 27 individual D-amino acids, D-peptides, and isomeric amino acid derivatives and suggested research needs in each of these areas. The described results provide a valuable record and resource for further progress on the multifaceted aspects of D-amino acids in food and biological samples.

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Comparison of derivatization and chromatographic methods for GC–MS analysis of amino acid enantiomers in physiological samples

Cited by 53 publications

References 26 publications

Enantiomeric Ratio of Amino Acids as a Tool for Determination of Aging and Disease Diagnostics by Chromatographic Measurement

Enantiomeric Ratio of Amino Acids as a Tool for Determination of Aging and Disease Diagnostics by Chromatographic Measurement

Electrophoretic Extraction and Proteomic Characterization of Proteins Buried in Marine Sediments

Nutritional and medicinal aspects of d-amino acids

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