Selective oxidation in vitro by myeloperoxidase of the N-terminal amine in apolipoprotein B-100
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چکیده
منابع مشابه
Selective oxidation in vitro by myeloperoxidase of the N-terminal amine in apolipoprotein B-100.
In contrast to the multiple low abundance 2,4-dinitrophenylhydrazine-reactive tryptic peptides formed by oxidation of LDL with reagent HOCl in vitro, myeloperoxidase-catalyzed oxidation produces a dominant product in considerably greater yield and selectivity. This modified peptide had a single amino-terminal sequence corresponding to amino acids 53-66 of apolipoprotein B-100 (apoB-100), but it...
متن کاملSelective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro.
Oxidative modification of LDL may be important in the initiation and/or progression of atherosclerosis, but the precise mechanisms through which low density lipoprotein (LDL) is oxidized are unknown. Recently, evidence for the existence of HOCl-oxidized LDL in human atherosclerotic lesions has been reported, and myeloperoxidase (MPO), which is thought to act through production of HOCl, has been...
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ژورنال
عنوان ژورنال: Journal of Lipid Research
سال: 2001
ISSN: 0022-2275
DOI: 10.1016/s0022-2275(20)31515-7