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Cross‐linking of collagen CNBr peptides by ozone or UV light
Author(s) -
Fujimori Eiji
Publication year - 1988
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(88)81241-9
Subject(s) - cyanogen bromide , chemistry , fluorescence , size exclusion chromatography , peptide , cyanogen , gel electrophoresis , chromatography , electrophoresis , ozone , biochemistry , peptide sequence , organic chemistry , enzyme , physics , quantum mechanics , gene
Insoluble collagen from rat tail tendon was digested with cyanogen bromide. The resultant peptides were dissolved in 0.1% SDS solution and separated by gel filtration and gel electrophoresis. Cross‐linking occurred in CNBr‐cleaved peptides when they were exposed to ozone or biologically effective UV (300 nm) radiation. The enhancement of a blue fluorescence at 430 nm (excited at 350 nm) was found to be associated with oxidized, cross‐linked peptides. Polymeric peptides, formed in collagen with aging, also exhibited enhanced blue fluorescence.