AFFINITY ELUTION FROM A PHOSPHONIC ACID SEPHAROSE DERIVATIVE IN THE PURIFICATION OF HUMAN-LIVER ALKALINE-PHOSPHATASE

被引：34

作者：

SEARGEANT, LE

STINSON, RA

机构：

[1] Medical Laboratory Science, Department of Pathology, University of Alberta, Edmonton

来源：

JOURNAL OF CHROMATOGRAPHY | 1979年 / 173卷 / 01期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/S0021-9673(01)80449-0

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The compound p-aminobenzylphosphonic acid has been coupled via an azo linkage to tyraminyl-Sepharose 4B. This derivative at pH 6.0 bound most of the protein and all of the alkaline phosphatase in a crude preparation from human liver. The phosphatase was selectively eluted with the substrate 2-naphthylphosphate and a purification of 400-fold obtained. This step, when incorporated into a procedure for the purification of human liver alkaline phosphatase, yielded essentially pure enzyme. © 1979.

引用

页码：101 / 108

页数：8

共 18 条

[1]

ALLEN RC, 1974, AM J CLIN PATHOL, V62, P732

[2] STRUCTURAL EVIDENCE THAT HUMAN LIVER AND PLACENTAL ALKALINE-PHOSPHATASE ISOENZYMES ARE CODED BY DIFFERENT GENES [J].