title: Covalent binding of peroxidized linoleic acid to protein and amino acids as models for lipofuscin formation.
abstract: The fluorescent substances produced by the reaction of linoleic acid hydroperoxides (LOOH) with ca. 20 different amino acids and bovine serum albumin (BSA) were studied. Only the amino acids, lysine, glycine, arginine, histidine and phenylalanine, gave products with strong fluorescent properties. Products of lysine had a fluorescence intensity of ca. 10 times those of glycine and 100 times those of phenylalanine. The N-acylation of amino acids greatly reduced the fluorescence of the products of the reaction except lysine and arginine. The fluorescence of the products of the reaction of LOOH with N-acetyl BSA was only ca. 25% of the control BSA under the same conditions. It appeared that the substances formed from the reaction of LOOH with BSA were crosslinked polymers as evidenced by column chromatography and polyacrylamide gel electrophoresis. These products were insoluble in common organic solvents and their fluorescent intensities correlated well with the thiobarbituric acid (TBA) test. These observations appear to be highly important in the formation of lipofuscin substances, particularly those associated with the aging pigments which accumulate during aging in mammalian tissues.
authors: Department of Biochemistry, Teikyo University School of Medicine, 2-11-1 Kaga, 173, Itabashi, Tokyo, Japan.
authors: H
authors: H
authors: Shimasaki
authors: Department of Biochemistry, Teikyo University School of Medicine, 2-11-1 Kaga, 173, Itabashi, Tokyo, Japan.
authors: N
authors: N
authors: Ueta
authors: The Hormel Institute, University of Minnesota, 55912, Austin, MN.
authors: O S
authors: OS
authors: Privett