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丝氨酸蛋白酶抑制剂与补体系统。

Serpins and the complement system.

作者信息

Beinrohr László, Murray-Rust Thomas A, Dyksterhuis Leanne, Závodszky Péter, Gál Péter, Pike Robert N, Wijeyewickrema Lakshmi C

机构信息

Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Hungary.

出版信息

Methods Enzymol. 2011;499:55-75. doi: 10.1016/B978-0-12-386471-0.00004-3.

DOI:10.1016/B978-0-12-386471-0.00004-3
PMID:21683249
Abstract

C1-inhibitor (serpin G1) is a 105 kDa inhibitor which functions as a major antiinflammatory protein in the body. It has its effects via inhibition of the proteases of the complement system and contact system of coagulation, as well as several direct effects mediated by its unique highly glycosylated N-terminal domain. The serpin controls a number of different proteases very efficiently and for some of these the function is augmented by the cofactor, heparin. Here, we describe the preparation of human plasma and recombinant C1-inhibitor and the basic methods required for their characterization, using the complement enzyme C1s as an example of a target enzyme.

摘要

C1抑制剂(丝氨酸蛋白酶抑制剂G1)是一种105 kDa的抑制剂,在体内作为主要的抗炎蛋白发挥作用。它通过抑制补体系统和凝血接触系统的蛋白酶发挥作用,以及通过其独特的高度糖基化的N端结构域介导的一些直接作用。该丝氨酸蛋白酶抑制剂能非常有效地控制多种不同的蛋白酶,对于其中一些蛋白酶,辅因子肝素可增强其功能。在此,我们以补体酶C1s作为靶酶的实例,描述人血浆和重组C1抑制剂的制备及其表征所需的基本方法。

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Serpins and the complement system.丝氨酸蛋白酶抑制剂与补体系统。
Methods Enzymol. 2011;499:55-75. doi: 10.1016/B978-0-12-386471-0.00004-3.
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Functional characterization of the recombinant human C1 inhibitor serpin domain: insights into heparin binding.重组人 C1 抑制剂丝氨酸蛋白酶抑制剂结构域的功能特征:肝素结合的深入了解。
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Expression of active human C1 inhibitor serpin domain in Escherichia coli.活性人C1抑制剂丝氨酸蛋白酶抑制剂结构域在大肠杆菌中的表达。
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Regulation of C1-inhibitor function by binding to type IV collagen and heparin.通过与IV型胶原蛋白和肝素结合对C1抑制剂功能进行调节。
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Polyphosphate is a novel cofactor for regulation of complement by a serpin, C1 inhibitor.多聚磷酸盐是丝氨酸蛋白酶抑制剂C1抑制剂调节补体的一种新型辅助因子。
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Heparin-stimulated modification of C1-inhibitor by subcomponent C1s of human complement.肝素刺激下人补体C1s亚成分对C1抑制物的修饰作用。
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The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant.一种病理性突变体表明,C1抑制剂丝氨酸蛋白酶抑制剂结构域的功能完整性取决于独特的N端结构域。
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Recombinant human C1-inhibitor produced in Pichia pastoris has the same inhibitory capacity as plasma C1-inhibitor.在毕赤酵母中产生的重组人C1抑制因子具有与血浆C1抑制因子相同的抑制能力。
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