Abstract
ROS, including (.)OH, is now recognized as the hallmark of inflammation and damage to the anti-proteinase barrier has been implicated in a number of pathophysiological conditions. We have previously shown that O2( -) and H2O2/HOCl are physiologically relevant inactivators of alpha 2M, a key anti-proteinase. Here, we show that (.)OH disrupted caprine alpha2M structure and antiproteolytic potential in vitro, suggesting that its function could be compromised via oxidative modification.
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