Immunological identification of the heart myoglobin radical formed by hydrogen peroxide

被引：101

作者：

Detweiler, CD

Deterding, LJ

Tomer, KB

Chignell, CF

Germolec, D

Mason, RP

机构：

[1] NIEHS, Lab Pharmacol & Chem, NIH, Res Triangle Pk, NC 27709 USA

[2] NIEHS, Struct Biol Lab, NIH, Res Triangle Pk, NC 27709 USA

[3] NIEHS, Toxicol Lab, NIH, Res Triangle Pk, NC 27709 USA

来源：

FREE RADICAL BIOLOGY AND MEDICINE | 2002年 / 33卷 / 03期

关键词：

myoglobin; 5,5-dimethyl-1-pyrroline N-oxide (DMPO); antibodies; protein radical; western blot; free radicals;

D O I：

10.1016/S0891-5849(02)00895-X

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：

This study reports the detection of protein free radicals using the specific free radical reactivity of nitrone spin traps in conjunction with nitrone-antibody specificity. Polyclonal antibodies were developed that bind to protein adducts of the nitrone spin-trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO). The antibodies were used to detect DMPO protein adducts produced on horse myoglobin resulting from self-peroxidation. Western blot analysis demonstrates that myoglobin forms the predominant radical-derived nitrone adduct in rat heart Supernatant. Published by Elsevier Science Inc.

引用

页码：364 / 369

页数：6

共 22 条

[1] ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide [J].