IMMUNOAFFINITY CHROMATOGRAPHIC PURIFICATION OF RUSSELL VIPER VENOM FACTOR-X ACTIVATOR USING ELUTION IN HIGH-CONCENTRATIONS OF MAGNESIUM-CHLORIDE

被引：26

作者：

DURKEE, KH

ROH, BH

DOELLGAST, GJ

机构：

[1] WAKE FOREST UNIV, BOWMAN GRAY SCH MED, DEPT BIOCHEM, MED CTR BLVD, WINSTON SALEM, NC 27157 USA

[2] ELCATECH INC, WINSTON SALEM, NC 27103 USA

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1993年 / 4卷 / 05期

关键词：

D O I：

10.1006/prep.1993.1053

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

RVV-X, the factor X activator from Russell′s viper venom, has been isolated using affinity chromatography on agarose columns of a monoclonal antibody specific for this enzyme. Upon testing acid, alkaline, and high concentrations of MgCl2 for elution, it was found that use of high concentrations of MgCl2 was most effective in elution of RVV-X. It was nondenaturing and yielded 90% recovery of homogeneous enzyme without measurable contamination by other proteins of the venom. © 1993 Academic Press. All rights reserved.

引用

页码：405 / 411

页数：7

共 25 条

[1] CATION BINDING-PROPERTIES OF THE MULTIPLE SUBFORMS OF RVV-X, THE COAGULANT PROTEIN FROM VIPERA-RUSSELLI [J].