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一种从牛血浆中同时分离因子X和凝血酶原的方法。

A method for the simultaneous isolation of factor X and prothrombin from bovine plasma.

作者信息

Esnouf M P, Lloyd P H, Jesty J

出版信息

Biochem J. 1973 Apr;131(4):781-9. doi: 10.1042/bj1310781.

Abstract
  1. A method is described for the simultaneous isolation of both Factor X and prothrombin from bovine plasma. The proteins are adsorbed on and eluted from barium sulphate and chromatographed on DEAE-Sephadex and are finally purified by rechromatography on DEAE-Sephadex. 2. The proteins can be purified in 48h from the collection of the blood and the method can be used to process large volumes of plasma. 3. The prothrombin has a molecular weight of 70300; the Factor X, on the other hand, is polydisperse, with most of the protein (86%) having a molecular weight of 56000.
摘要
  1. 本文描述了一种从牛血浆中同时分离因子X和凝血酶原的方法。这些蛋白质先吸附于硫酸钡上,然后洗脱,接着在二乙氨基乙基葡聚糖凝胶(DEAE - Sephadex)上进行色谱分离,最后通过在DEAE - Sephadex上再次色谱分离进行纯化。2. 从采血开始,这些蛋白质可在48小时内得到纯化,该方法可用于处理大量血浆。3. 凝血酶原的分子量为70300;另一方面,因子X具有多分散性,大部分蛋白质(86%)的分子量为56000。

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Preparation of bovine blood coagulation factors X1 and X2.牛凝血因子X1和X2的制备。
Biol Chem Hoppe Seyler. 1985 Dec;366(12):1103-8. doi: 10.1515/bchm3.1985.366.2.1103.
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Purification and characterization of human Factor II.人凝血因子II的纯化与特性分析
Biochim Biophys Acta. 1973 Mar 30;304(1):103-13. doi: 10.1016/0304-4165(73)90119-0.

本文引用的文献

9
Purification and properties of bovine prothrombin.牛凝血酶原的纯化及特性
Biochemistry. 1969 May;8(5):1860-9. doi: 10.1021/bi00833a013.

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