Identification of Nε-(carboxyethyl)lysine, one of the methylglyoxal-derived AGE structures, in glucose-modified protein:: mechanism for protein modification by reactive aldehydes

被引：34

作者：

Nagai, R

Araki, T

Hayashi, CM

Hayase, F

Horiuchi, S

机构：

[1] Kumamoto Univ, Sch Med, Dept Biochem, Kumamoto 8600811, Japan

[2] Kyushu Tokai Univ, Fac Agr, Kumamoto, Japan

[3] Meiji Univ, Dept Agr Chem, Kawasaki, Kanagawa 214, Japan

来源：

JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2003年 / 788卷 / 01期

基金：

日本学术振兴会;

关键词：

Maillard reaction; N-epsilon-(carboxyethyl)lysine; N-epsilon-(carboxymethyl)lysine; proteins; aldehydes;

D O I：

10.1016/S1570-0232(02)01019-X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

We have developed a separation system for N-epsilon-(carboxyethyl)lysine (CEL) and N-epsilon-(carboxymethyl)lysine (CML) by HPLC equipped with a styrene-divinylbenzene copolymer resin coupled with sulfonic group cation-exchange column and examined whether CEL is formed from proteins modified by glucose via the Maillard reaction. CEL was generated by incubating bovine serum albumin (BSA) with glucose, a reaction inhibited by aminoguanidine, but enhanced by phosphate. Although several aldehydes were detected during incubation of N-alpha-acetyllysine with glucose, incubation of BSA with methylglyoxal alone generated CEL. These results indicate that methylglyoxal is responsible for CEL formation on protein in vitro. (C) 2003 Elsevier Science B.V. All rights reserved.

引用

页码：75 / 84

页数：10

共 32 条

[1] N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins [J].