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23. Krause, R., Schlegel, K., Schwarzer, E., Henle, T. (2008). Studies on the formation of peptide-bound Heyns compounds. J. Agric. Food Chem., 56, 2522 2527. 24. Eichner, K. (1982). Analytical detection of thermally induced qualitative changes in vegetables and fruits. Z. Lebensm. Unters. Forsch., 36, 101 104. 25. Wittmann, R., Eichner, K. (1989). Detection of Maillard products in malts, beers, and brewing colorants. Z. Lebensm. Unters. Forsch., 188, 212 220. 26. Sanz, M.L., del Castillo, M.D., Corzo, N., Olano, A. (2003). 2-Furoylmethyl amino acids and hydroxymethylfurfural as indicators of honey quality. J. Agric. Food Chem., 51, 4278 4283. 27. Anet, E.F.L.J. (1960). Degradation of carbohydrates I. Isolation of 3deoxyhexosones. Aust. J. Chem., 13, 396 403. 28. Glomb, M.A., Pfahler, C. (2000). Synthesis of 1-deoxy-D-erythro-hexo-2,3-diulose, a major hexose Maillard intermediate. Carbohydr. Res., 329, 515 523. 29. Pischetsrieder, M., Schroeter, C., Severin, T. (1998). Formation of an aminoreductone during the Maillard reaction of lactose with N-alpha-acetyllysine or proteins. J. Agric. Food Chem., 46, 928 931. 30. Mavric, E., Kumpf, Y., Schuster, K., Kappenstein, O., Scheller, D., Henle, T. (2004). A new imidazolinone resulting from the reaction of peptide-bound arginine and oligosaccharides with 1,4-glycosidic linkages. Eur. Food Res. Technol., 218, 213 218. 31. Belitz, H.D., Grosch, W., Schieberle, P. (2004). Food Chemistry, 3rd edn, Springer. 32. Hollnagel, A., Kroh, L.W. (2000). Degradation of oligosaccharides in nonenzymatic browning by formation of alpha-dicarbonyl compounds via a peeling off mechanism. J. Agric. Food Chem., 48, 6219 6226. 33. Berg, H.E., van Boekel, M.A.J.S. (1994). Degradation of lactose during heating of milk. Neth. Milk Dairy J., 48, 157 175. 34. Ahmed, M.U., Dunn, J.A., Walla, M.D., Thorpe, S.R., Baynes, J.W. (1986). Identi cation of N-epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J. Biol. Chem., 263, 8816 8821. 35. B ser, W., Erbersdobler, H. (1986). Carboxymethyllysine, a new compound of heat damage in milk products. Milchwissenschaft, 41, 780 785. 36. Kasper, M., Schieberle, P. (2005). Labelling studies on the formation pathway of N-epsilon-carboxymethyllysine in Maillard-type reactions. Ann. N. Y. Acad. Sci., 1043, 59 62. 37. Fu, M.X., Requena, J.R., Jenkins, A.J., Lyons, T.J., Baynes, J.W., Thorpe, S.R. (1996). The advanced glycation end product, N-epsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. J. Biol. Chem., 271, 9982 9986. 38. Nakayama, T., Hayase, F., Kato, H. (1980). Formation of epsilon-(2-formyl-5hydroxy-methyl-pyrrol-1-yl)-L-norleucin in the Maillard reaction between Dglucose and L-lysine. Agric. Biol. Chem., 44, 1201 1202. 39. Henle, T., Walter, A.W., Klostermeyer, H. (1994). Simultaneous determination of protein-bound Maillard products by ion-exchange chromatography and photodiode array detection, in Maillard Reactions in Chemistry, Food and Health (eds
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T.P. Labuza, G.A. Reineccius, V.M. Monnier, J. O Brien, J.W. Baynes), The Royal Society of Chemistry, pp. 195 200. Henle, T., Bachmann, A. (1996). Synthesis of pyrraline. Z. Lebensm. Unters. Forsch., 202, 72 75. Henle, T., Klostermeyer, H. (1993). Determination of protein-bound 2-amino6-(2-formyl-2-hydroxymethyl-1-pyrrolyl)-hexanoic acid ( pyrraline ) by ionexchange chromatography and photodiode array detection. Z. Lebensm. Unters. Forsch., 196, 1 4. Lindenmeier, M., Faist, V., Hofmann, T. (2002). Structural and functional characterization of pronyl-lysine, a novel protein modi cation in bread crust melanoidins showing in vitro antioxidative and phase I/II enzyme modulating activity. J. Agric. Food Chem., 50, 6997 7006. Cho, R.K., Okitani, A., Kato, H. (1986). Polymerization of proteins and impairment of their arginine residues due to intermediate compounds in the Maillard reaction. Dev. Food Sci., 13, 439 448. Kato, Y., Matsuda, T., Kato, N., Nakamura, R. (1988). Browning and protein polymerization induced by amino-carbonyl reaction of ovalbumin with glucose and lactose. J. Agric. Food Chem., 36, 806 809. Sell, D.R., Monnier, V.M. (1991). Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. J. Biol. Chem., 264, 21597 21602. Henle, T., Schwarzenbolz, U., Klostermeyer, H. (1997). Detection and quanti cation of pentosidine in foods. Z. Lebensm. Unters. Forsch., 204, 95 98. Biemel, K.M., Reihl, O., Conrad, J., Lederer, M.O. (2001). Formation pathways for lysine-arginine cross-links derived from hexoses and pentoses by Maillard processes: unraveling the structure of a pentosidine precursor. J. Biol. Chem., 276, 23405 23412. Henle, T., Walter, A.W., Haessner, R., Klostermeyer, H. (1994). Isolation and identi cation of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal. Z. Lebensm. Unters. Forsch., 199, 55 58. Ahmed, N., Argirov, O.K., Minhas, H.S., Cordeiro, C.A., Thornalley, P.J. (2002). Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N-hydroxysuccinimidylcarbamate and application to N-epsilon-carboxymethyl-lysine- and N-epsilon-(1-carboxyethyl)lysine-modi ed albumine. Biochem. J., 364, 1 14. Thornalley, P.J., Battah, S., Ahmed, N., Karachalias, N., Agalou, S., Babaei-Jadidi, R., Dawnay, A. (2003). Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry. Biochem. J., 375, 581 592. Schwarzenbolz, U., Henle, T., Haessner, R., Klostermeyer, H. (1997). On the reaction of glyoxal with proteins. Z. Lebensm. Unters. Forsch., 205, 121 124. Konishi, Y., Hayase, F., Kato, H. (1994). Novel imidazolone compound formed by the advanced Maillard reaction of 3-deoxyglucosone and arginine residues in proteins. Biosci. Biotech. Biochem., 58, 1953 1955. Shipanova, I.N., Glomb, M.A., Nagaraj, R.H. (1997). Protein modi cation by methylglyoxal: chemical nature and synthetic mechanism of a major uorescent adduct. Arch. Biochem. Biophys., 344, 29 36.
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