RAPID PURIFICATION OF IMMUNOGLOBULIN-G USING AZA-ARENOPHILIC CHROMATOGRAPHY - NOVEL MODE OF PROTEIN SOLID-PHASE INTERACTIONS

被引：9

作者：

NGO, TT ^{[1
]}

机构：

[1] UNIV CALIF IRVINE, DEPT DEV & CELL BIOL, IRVINE, CA 92717 USA

来源：

JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 1994年 / 662卷 / 02期

关键词：

D O I：

10.1016/0378-4347(94)00251-7

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A derivative of aza-arenophilic gel having a dichlorosubstituent and an hydroxy ion as a capping nucleophile has been prepared. The properties of this gel in relation to IgG purification have been investigated in details. In the presence of high salt (1.5 M), albumin and some other serum proteins did not bind to the gel. IgG and some other minor proteins, however, were bound to the gel. The bound proteins can be eluted with an acidic buffer. SDS-PAGE showed that the fraction eluted with 0.1 M sodium acetate pH 4.2 consisted mainly of IgGs.

引用

页码：351 / 356

页数：6

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