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Hydroxyl Radical Mediates Oxidative Modification of Caprine Alpha-2 Macroglobulin

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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 α2M, a key anti-proteinase. Here, we show that .OH disrupted caprine α2M structure and antiproteolytic potential in vitro, suggesting that its function could be compromised via oxidative modification.

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Keywords: Caprine; alpha-2-macroglobulin; hydroxyl radical

Document Type: Research Article

Publication date: 01 January 2009

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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