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Non‐enzymatic glycation of histones
Author(s) -
Liebich H. M.,
Gesele E.,
Wirth C.,
Wöl J.,
Jobst K.,
Lakatos A.
Publication year - 1993
Publication title -
biological mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1052-9306
DOI - 10.1002/bms.1200220204
Subject(s) - histone , glycation , lysine , chemistry , biochemistry , enzyme , in vitro , hydrolysis , chromatography , amino acid , dna , receptor
2‐(2‐Furoyl)‐5‐(2‐furanyl)‐1 H ‐imidazole (FFI) is detected in total histones and the lysine‐rich histone 1 fraction isolated from calf thymus after in vitro glycation and hydrolysis with HCl, using gas chromatographic/mass spectrometric analysis. The finding suggests that glucose is bound to the ϵ‐amino groups of the lysine residues of the histones. No FFI is monitored in native histone samples.