Abstract
γ-Glutamyl semialdehyde is a primary oxidation product of apolipoprotein (apo) B-100 proline (Pro) and arginine (Arg) side chain residues. By reduction γ-glutamyl semialdehyde forms 5-hydroxy-2-aminovaleric acid (HAVA). Here we describe the application of sensitive and specific HAVA measurement to characterize the formation of γ-glutamyl semialdehyde in several domains of apoB-100 in LDL 1 (S f 7–12) and LDL 2 (S f 0–7) subfractions subjected to oxidative damage in the presence of iron in vitro. Results suggest that susceptibility of apoB-100 Pro and Arg residues toward oxygen radicals drastically changes along the lipoprotein metabolic cascade.
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