Wasil M, Halliwell B, Hutchison D C, Baum H
Biochem J. 1987 Apr 1;243(1):219-23. doi: 10.1042/bj2430219.
The elastase-inhibitory capacity of purified human alpha 1-antiproteinase is inactivated by low concentrations of the myeloperoxidase-derived oxidant hypochlorous acid, but much higher concentrations are required to inhibit the elastase-inhibitory capacity of serum samples. The protective effect of serum appears to be largely due to albumin. High concentrations of H2O2 also inactivate the elastase-inhibitory capacity of alpha 1-antiproteinase, by a mechanism not involving formation of hydroxyl radicals. Serum offers protection against H2O2 inactivation of alpha 1-antiproteinase. The relevance of these results to the tissue damage produced by activated phagocytes is discussed.
纯化的人α1抗蛋白酶的弹性蛋白酶抑制能力可被低浓度的髓过氧化物酶衍生的氧化剂次氯酸灭活,但需要高得多的浓度才能抑制血清样本的弹性蛋白酶抑制能力。血清的保护作用似乎主要归因于白蛋白。高浓度的H2O2也会通过不涉及羟基自由基形成的机制使α1抗蛋白酶的弹性蛋白酶抑制能力失活。血清可提供针对H2O2使α1抗蛋白酶失活的保护作用。讨论了这些结果与活化吞噬细胞产生的组织损伤的相关性。