Purification and properties of bovine prothrombin.

Purification and properties of bovine prothrombin.
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牛凝血酶原的纯化和性质。

DOI:
10.1021/bi00833a013
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发表时间:
1969
期刊:
影响因子:
2.9
通讯作者:
H. Scheraga
H. Scheraga
中科院分区:
生物学3区
文献类型:
--
作者:
J. Ingwall;H. Scheraga

文献摘要

被引文献

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Joanne S. Ingwallf和Harold A. Scheragação摘要:本文报道了一种快速、简便、重复性好的纯化牛凝血酶原的方法。通过进行等电沉淀,DEAE-Sephadex层析,和超离心,以18%的产率,无污染物的圆盘凝胶电泳的灵敏度标准进行评估,得到的产品。进行化学和物理化学表征研究以确定分子的大小和形状。凝血酶原在磷酸盐缓冲液中的沉降平衡分子量为74,000 ±4100,沉降系数为4.80 S,特性粘度为3.4 cc/g,粘度值为2.07 X 106,pos-
Joanne S. Ingwallf and Harold A. ScheragaÍ abstract: A rapid, simple, and reproducible method for the purification of bovine prothrombin, starting with a commercial preparation, is reported. By carrying out isoelectric precipitation, chromatography on DEAE-Sephadex, and ultracentrifugation, a product in 18% yield, free of contaminants as evaluated by the sensitive criterion of disc gel electrophoresis, was obtained. Chemical and physiocochemical characterization studies were performed to determine the size and shape of the molecule. Prothrombin in phosphate buffer has a sedi-mentation equilibrium molecular weight of 74,000±4100, a sedimentation coefficient of 4.80 S, intrinsic viscosity of 3.4 cc/g, a value for ß of 2.07 X 106, pos-