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Different susceptibility to oxidation of proline and arginine residues of apolipoprotein B‐100 among subspecies of low density lipoproteins
Author(s) -
Pietzsch Jens,
Julius Ulrich
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02181-0
Subject(s) - arginine , subspecies , chemistry , apolipoprotein b , proline , biochemistry , food science , amino acid , biology , cholesterol , zoology
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.