Determination of theMaillard product oxalic acidmonolysinylamide (OMA) in heated milk products by ELISA

Hasenkopf, Katrin; Übel, B.; Bordiehn, T.; Pischetsrieder, Monika

doi:10.1002/1521-3803(20010601)45:3<206::aid-food206>3.0.co;2-1

Cited by 12 publications

(11 citation statements)

References 19 publications

(27 reference statements)

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“…Oxalic acid monolysinylamide (OMA), a MRP of l-ascorbic acid, was detected in heat-treated milk products and commercial infant formulas using ELISA [147][148][149]. In this qualitative assay, a polyclonal antibody, which binds with high specificity and affinity to OMA-modified proteins, was used.…”

Section: Analysis Of Other Amino Acid Derivativesmentioning

confidence: 99%

Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods

Silván

Lagemaat

Olano

et al. 2006

Journal of Pharmaceutical and Biomedical Analysis

157

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Section: Analysis Of Other Amino Acid Derivativesmentioning

confidence: 99%

Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods

Silván

Lagemaat

Olano

et al. 2006

Journal of Pharmaceutical and Biomedical Analysis

157

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“…Samples were analyzed in triplicates. One Unit equals inhibition obtained with 1 µg/mL of CML-HSA or synthesized imidazolone-HSA (9).…”

Section: Chemicalsmentioning

confidence: 99%

“…To date, several techniques are applied for the detection and quantification of protein glycation products. Apart from chromatographic techniques including gas (7) and liquid chromatography (8), immmunochemical methods, mainly competitive ELISA (9), are used. Either of these techniques use secondary properties of particular Maillard products, such as fluorescence, UV-absorption, or affinity to highly specific antibodies, for identification and quantification.…”

Section: Introductionmentioning

confidence: 99%

Relative Quantification of N^ε-(Carboxymethyl)lysine, Imidazolone A, and the Amadori Product in Glycated Lysozyme by MALDI-TOF Mass Spectrometry

Kislinger

Humeny

Peich

et al. 2002

J. Agric. Food Chem.

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The nonenzymatic glycation of proteins by reducing sugars, also known as the Maillard reaction, has received increasing recognition from nutritional science and medical research. In this study, we applied matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) to perform relative and simultaneous quantification of the Amadori product, which is an early glycation product, and of N(epsilon)-(carboxymethyl)lysine and imidazolone A, two important advanced glycation end products. Therefore, native lysozyme was incubated with d-glucose for increasing periods of time (1, 4, 8, and 16 weeks) in phosphate-buffered saline pH 7.8 at 50 degrees C. After enzymatic digestion with endoproteinase Glu-C, the N-terminal peptide fragment (m/z 838; amino acid sequence KVFGRCE) and the C-terminal peptide fragment (m/z 1202; amino acid sequence VQAWIRGCRL) were used for relative quantification of the three Maillard products. Amadori product, N(epsilon)-(carboxymethyl)lysine, and imidazolone A were the main glycation products formed under these conditions. Their formation was dependent on glucose concentration and reaction time. The kinetics were similar to those obtained by competitive ELISA, an established method for quantification of N(epsilon)-(carboxymethyl)lysine and imidazolone A. Inhibition experiments showed that coincubation with N(alpha)-acetylargine suppressed formation of imidazolone A but not of the Amadori product or N(epsilon)-(carboxymethyl)lysine. The presence of N(alpha)-acetyllysine resulted in the inhibition of lysine modifications but in higher concentrations of imidazolone A. o-Phenylenediamine decreased the yield of the Amadori product and completely inhibited the formation of N(epsilon)-(carboxymethyl)lysine and imidazolone A. MALDI-TOF-MS proved to be a new analytical tool for the simultaneous, relative quantification of specific products of the Maillard reaction. For the first time, kinetic data of defined products on specific sites of glycated protein could be measured. This characterizes MALDI-TOF-MS as a valuable method for monitoring the Maillard reaction in the course of food processing.

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“…Furthermore, immunochemical methods have been successfully applied for analysis (9). In the course of these studies, various protein glycation products have been identified in model mixtures or in heated foodstuffs, and include the Amadori product, N -(carboxymethyl)lysine (1) (10), oxalic acid mono-N -lysinylamide (2) (11), pentosidine (12), or pyrraline (13). N -(carboxymethyl)lysine and oxalic acid mono-N -lysinylamide (9)(10)(11) have been used as markers for heat treatment of different food products.…”

Section: Introductionmentioning

confidence: 99%

Analysis of Glycated and Ascorbylated Proteins by Gas Chromatography−Mass Spectrometry

Hasenkopf

Rönner

Hiller

et al. 2002

J. Agric. Food Chem.

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Proteins or poly-L-lysine which were incubated in the presence of ascorbic acid, dehydroascorbic acid (ascorbylation), or various sugars (glycation) were analyzed by gas chromatography-mass spectrometry (GC-MS). To also detect more labile reaction products, the Maillard modified proteins or poly-L-lysine were enzymatically hydrolyzed and reacted with N-methyl-N-(tert-butyldimethylsilyl)trifluoroacetamide to form the N(O)-tert-butyldimethylsilyl (tBDMS) derivatives prior to GC analysis. Under these conditions, the known Maillard products N (epsilon)-(carboxymethyl)lysine (1), oxalic acid mono-N (epsilon)-lysinylamide (2), and N (epsilon)-(carboxyethyl)lysine (3) could be simultaneously detected and quantified in glycated and ascorbylated proteins. Additionally, N (epsilon)-(1-carboxy-3-hydroxypropyl)-L-lysine (4) was identified for the first time as a Maillard product of proteins. Under the conditions applied here, 4 was found only in ascorbylated proteins or poly-L-lysine, but not in glycated proteins. Maillard-modified poly-L-lysine was further subjected to high-performance liquid chromatography (HPLC) analysis after enzymatic hydrolysis and formation of the phenyl isothiocyanate derivatized amino acids. Using this method, N (epsilon)-formyl-L-lysine (5), which cannot be distinguished from 2 by GC-MS analysis, was identified for the first time as a glycation product. Compound 5 is mainly formed from ribose, lactose, and fructose. The indicated Maillard products were quantified in beta-lactoglobulin (GC-MS) or poly-L-lysine (HPLC) which were glycated or ascorbylated using different precursors.

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Determination of theMaillard product oxalic acidmonolysinylamide (OMA) in heated milk products by ELISA

Cited by 12 publications

References 19 publications

Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods

Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods

Relative Quantification of N^ε-(Carboxymethyl)lysine, Imidazolone A, and the Amadori Product in Glycated Lysozyme by MALDI-TOF Mass Spectrometry

Analysis of Glycated and Ascorbylated Proteins by Gas Chromatography−Mass Spectrometry

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Determination of theMaillard product oxalic acidmonolysinylamide (OMA) in heated milk products by ELISA

Cited by 12 publications

References 19 publications

Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods

Analysis and biological properties of amino acid derivates formed by Maillard reaction in foods

Relative Quantification of Nε-(Carboxymethyl)lysine, Imidazolone A, and the Amadori Product in Glycated Lysozyme by MALDI-TOF Mass Spectrometry

Analysis of Glycated and Ascorbylated Proteins by Gas Chromatography−Mass Spectrometry

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Relative Quantification of N^ε-(Carboxymethyl)lysine, Imidazolone A, and the Amadori Product in Glycated Lysozyme by MALDI-TOF Mass Spectrometry