Analysis of carboxymethyl-lysine in AGE-protein of the Maillard reaction

International Congress Series

Volumn 1223, Issue C, 2001, Pages 59-64

  Araki, Tomohiro ^a   Nagai, Ryoji ^b   Araki, Norie ^b   Horiuchi, Seikoh ^b  

^a TOKAI UNIVERSITY   (Japan)

^b KUMAMOTO UNIV SCHOOL OF MEDICINE   (Japan)

Author keywords

Amino acid analysis; Glycation

Indexed keywords

EID: 79954418436     PISSN: 05315131     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0531-5131(01)00452-6     Document Type: Article

References (6)

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2. K. Yamada H. Nakano M. Nakayama O. Nozaki Y. Miura S. Suzuki H. Tuchida N. Mimura N. Araki S. Horiuchi Immunohistochemical study of human advanced glycosylation end-products (AGE) in chronic renal failure Clin. Nephrol. 42 1994 354 361
3. M.A. Glomb V.M. Monnier Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction J. Biol. Chem. 270 1995 10017 10026
4. M.U. Ahmed E. Brinkmann T.P. Degenhardt S.R. Thorpe J.W. Baynes Epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins Biochem. J. 324 1997 565 570
5. M.C. Wells-Knecht S.R. Thrope J.W. Baynes Pathways of formation of glycoxidation products during glycation of collagen Biochemistry 34 1995 15131 15141
6. N. Araki N. Ueno B. Chakrabarti Y. Morino S. Horiuchi Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging J. Biol. Chem. 267 1992 10211 10214