氧化型α-1-蛋白酶抑制剂的酶促还原可恢复其生物活性。
Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity.
作者信息
Abrams W R, Weinbaum G, Weissbach L, Weissbach H, Brot N
出版信息
Proc Natl Acad Sci U S A. 1981 Dec;78(12):7483-6. doi: 10.1073/pnas.78.12.7483.
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.
蛋白水解活性的主要血清抑制剂α-1-蛋白酶抑制剂（α-1-PI），（或α-1-抗胰蛋白酶）可通过氧化轻易失活[卡普，H.和贾诺夫，A.（1978年）《美国呼吸疾病评论》118，617 - 621]。这种失活似乎是由于α-1-PI中一个关键甲硫氨酸的氧化，而该甲硫氨酸是抑制弹性蛋白酶活性所必需的。一种来自大肠杆菌的可还原蛋白质中甲硫氨酸亚砜残基的酶[布罗特，N.、魏斯巴赫，L.、韦思，J.和魏斯巴赫，H.（1981年）《美国国家科学院院刊》78，2155 - 2158]能够恢复犬氧化α-1-PI的生物抑制活性。
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