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Structural And Functional Modifications Of Human Serum Albumin By Lipid Peroxidation By-Products, Amy Pollock
Structural And Functional Modifications Of Human Serum Albumin By Lipid Peroxidation By-Products, Amy Pollock
Electronic Theses and Dissertations
By-products of lipid peroxidation, specifically alpha, beta-unsaturated aldehydes, are known to modify nucleophilic amino acid residues, including lysine residues, in proteins. The produced alpha, beta-unsaturated aldehydes are stable enough to migrate from their site of origin, therefore allowing them to come in contact with a wide range of biomolecules in the system. Human serum albumin (HSA) is the most abundant plasma protein. It contains 58 lysine residues that are distributed throughout the sequence and tertiary structure of the protein, several of which are surface exposed. The research presented herein explores the possibility that HSA provides an outlet of consumption for …
Isolation And Characterization Of Water-Soluble Fluorescent Species From Human Serum, Ashraf Hamid Elamin
Isolation And Characterization Of Water-Soluble Fluorescent Species From Human Serum, Ashraf Hamid Elamin
Electronic Theses and Dissertations
Lipid peroxidation (LP) proceeds by a free radical chain reaction mechanism in which molecular oxygen is incorporated into polyunsaturated fatty acids (PUFA) to yield lipid hydroperoxides (LOOH). The ultimate end-products of LP are the production of alpha, beta unsaturated aldehydes, such as acrolein, 4-hydroxy-2-nonenal (HNE) and malondialdehyde (MDA). These aldehydes are very reactive and exhibit facile reactivity with various biomolecules, particularly proteins, resulting in the formation of fluorescent adducts that could be useful biological marker in diseases. These fluorescent adducts typically emit light between 400 and 600 nm when excited at wavelengths ranging from 300-400 nm. Lysine residues are the …