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C1酯酶抑制剂在激活C1r中的作用,C1r是来自人血浆的补体第一成分的一个亚组分。

The role of C1 esterase inhibitor in the activation of C1r, a subcomponent of the first component of complement from human plasma.

作者信息

Tamura Y, Okamura K, Otsuka A, Fujii S

出版信息

J Biochem. 1976 Feb;79(2):313-9. doi: 10.1093/oxfordjournals.jbchem.a131074.

Abstract

Clr was isolated from human serum by DEAE-cellulose column chromatography in the presence of EDTA. The isolated Clr did not hydrolyze N(alpha)-acetyl-L-arginine methyl ester, unless activated by brief treatment with trypsin [EC 3.4.21.4]. On thecolumn, the C1 esterase inhibitor activity was found to coincide with Clr but not C1s (another subcomponent of the first component) C1r was isolated from the euglobulin fraction of human serum by DEAE-cellulose column chromatograph. On Sephadex G-200 column chromatography, Clr was eluted in the void volume, whereas Clr was eluted in a position corresponding to a molecular weight of 140,000-160,000. The results indicated that, on activation, Clr was converted to an enzyme of lower molecular weight...

摘要

在EDTA存在的情况下,通过DEAE - 纤维素柱色谱法从人血清中分离出Clr。分离出的Clr不会水解N(α) - 乙酰 - L - 精氨酸甲酯,除非用胰蛋白酶[EC 3.4.21.4]进行短暂处理将其激活。在柱上,发现C1酯酶抑制剂活性与Clr一致,而与C1s(第一成分的另一个亚成分)不一致。通过DEAE - 纤维素柱色谱法从人血清的优球蛋白组分中分离出C1r。在Sephadex G - 200柱色谱上,Clr在空体积中被洗脱,而C1r在对应于分子量为140,000 - 160,000的位置被洗脱。结果表明,激活后,Clr转化为较低分子量的酶……

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