文章基本信息

标题：Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity
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作者：W R Abrams ; G Weinbaum ; L Weissbach 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：12
页码：7483-7486
DOI：10.1073/pnas.78.12.7483
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The major serum inhibitor of proteolytic activity, alpha-1-proteinase inhibitor (alpha-1-PI), (or alpha-1-antitrypsin) can be readily inactivated by oxidation [Carp, H. & Janoff, A. (1978) Am. Rev. Resp. Dis. 118, 617-621]. This inactivation appears to be due to the oxidation of a critical methionine(s) in alpha-1-PI that is required for the inhibition of elastase activity. An enzyme from Escherichia coli that reduces methionine sulfoxide residues in protein [Brot, N., Weissbach, L., Werth, J. & Weissbach, H. (1981) Proc. Natl. Acad. Sci. USA 78, 2155-2158] can restore the biological inhibitory activity of canine oxidized alpha-1-PI.