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2‐Oxo‐histidine as a novel biological marker for oxidatively modified proteins
Author(s) -
Uchida Koji,
Kawakishi Shunro
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80632-5
Subject(s) - histidine , chemistry , high performance liquid chromatography , radical , hydrolysis , derivative (finance) , biochemistry , chromatography , amino acid , financial economics , economics
We report a promising finding that oxidative modification of proteins by free radicals could be monitored by the formation of oxidized histidine that is detectable by reverse‐phase HPLC with electrochemical detection (HPLC‐ECD). When the N ‐protected histidine derivative ( N ‐benzoyl‐histidine) was exposed to a free radical‐generating system (copper/ascorbate), a number of products were detected by HPLC‐ECD and the main product among them was found to be identical to N ‐benzoyl‐2‐oxo‐histidine. The acid hydrolysis of N ‐benzoyl‐2‐oxo‐histidine provided a single product (2‐oxo‐histidine) that was detected sensitively by HPLC‐ECD. Thus 2‐oxo‐histidine was indeed generated as the main product in the oxidatively modified proteins by free radicals. Taken together, 2‐oxo‐histidine may be a useful biological marker for assessing protein modifications under oxidative stress.