Reduction of lipid hydroperoxides by apolipoprotein B-100

被引：12
作者：
Mashima, R
Yoshimura, S
Yamamoto, Y
机构：
[1] Univ Tokyo, Adv Sci & Technol Res Ctr, Meguro Ku, Tokyo 1538904, Japan
[2] Tokai Univ, Sch Med, Dept Mol Life Sci 2, Kanagawa 2591193, Japan
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 259卷 / 01期
关键词：
apolipoprotein B-100; phosphatidylcholine; hydroperoxide; phosphatidylcholine hydroxide; methionine; methionine sulfoxide; low density lipoprotein;
D O I：
10.1006/bbrc.1999.0739
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
We have previously isolated two proteins which can reduce phosphatidylcholine hydroperoxide (PC-OOH) from human blood plasma and identified one of the proteins as apolipoprotein A-I (Mashima, R., et al. (1998) J. Lipid Res. 39, 1133-1140), In the present study we have identified the other protein as apolipoprotein B-100 (apo B-100) by amino acid sequence analysis of its tryptic peptides. The reactivity of lipid hydroperoxides with apo B-100 decreased in the order of PC-OOH > linoleic acid hydroperoxide > cholesteryl ester hydroperoxide under our experimental conditions. Pretreatment of apo B-100 with chloramine T, an oxidant of methionine, diminished the PC-OOH-reducing activity, indicating that some of 78 methionines are responsible for the reduction of PC-OOH. Despite the presence of 6 methionines in albumin, albumin was inactive to reduce PC-OOH. Free methionine was also inactive. These data suggest that the accessibility and binding of lipid hydroperoxides to the protein methionine residues are crucial for reduction of lipid hydroperoxides. (C) 1999 Academic Press.
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页码：185 / 189
页数：5
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