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[从人血浆中纯化激肽原I和II并进行酶学研究]

[Purification and enzyme study of kininogens I and II from human plasma].

作者信息

Díaz A, Henriques O B

出版信息

Acta Physiol Lat Am. 1976;26(4):248-53.

PMID:1032268
Abstract

Kininogens I (HMW) and II (LMW) were isolated and partially purified from human plasma. The disappearance of kininogen I was prevented by the use of hexadimethrine bromide, which inhibits the activation of plasma prekallikrein. The two kininogens were separated by chromatography on DEAE-cellulose. Further purification of kininogen I and II was achieved by separate chromatographic steps of the partially purified kininogens on SP-Sephadex. The purification of the kininogens was controlled by incubation of the respective samples with different kininogenases: human plasma kallikrein, human salivary kallikrein and trypsin. As determined by gel filtration, a molecular weight of 250 000 daltons was found for kininogen I (HMW) and 48 000 daltons for kininogen II (LMW).

摘要

从人血浆中分离并部分纯化了激肽原I(高分子量)和II(低分子量)。使用抑制血浆前激肽释放酶激活的溴化六甲双铵可阻止激肽原I的消失。通过在DEAE - 纤维素上进行色谱分离将两种激肽原分开。通过将部分纯化的激肽原在SP - 葡聚糖凝胶上进行单独的色谱步骤,进一步纯化了激肽原I和II。通过将各个样品与不同的激肽原酶(人血浆激肽释放酶、人唾液激肽释放酶和胰蛋白酶)一起孵育来控制激肽原的纯化。通过凝胶过滤测定,发现激肽原I(高分子量)的分子量为250000道尔顿,激肽原II(低分子量)的分子量为48000道尔顿。

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