Fluorescent modification of serum albumin by lipid peroxidation

Abstract
Peroxidation of fatty acids bound to human serum albumin results in the production of fluorescent chromophores in the protein when it is stored in the liquid, powdered or crystalline state. Peroxidizing polyunsaturated fatty acid esters, and carbonyls derived from peroxidizing lipids react with amino groups of protein to give products that have fluorescence spectra very similar to those observed for stored commercial preparations of serum albumin.