Cross-linking of collagen CNBr peptides by ozone or UV light.
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.
Fujimori
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Department of Fine Structure Research, Boston Biomedical Research Institute, MA 02114.
D000818:Animals; D002850:Chromatography, Gel; D003094:Collagen / Q000528:radiation effects; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010126:Ozone; D011108:Polymers; D051381:Rats; D013050:Spectrometry, Fluorescence; D014466:Ultraviolet Rays
D011108:Polymers; D010126:Ozone; D003094:Collagen; D003488:Cyanogen Bromide