ISOLATION OF AN ARABINOGALACTAN PROTEIN BY LECTIN AFFINITY CHROMATOGRAPHY ON TRIDACNIN-SEPHAROSE-4B

被引：18

作者：

GLEESON, PA ^{[1
]}

JERMYN, MA ^{[1
]}

CLARKE, AE ^{[1
]}

机构：

[1] UNIV MELBOURNE,SCH BOT,PARKVILLE 3052,VICTORIA,AUSTRALIA

来源：

ANALYTICAL BIOCHEMISTRY | 1979年 / 92卷 / 01期

关键词：

D O I：

10.1016/0003-2697(79)90622-5

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

An arabinogalactan protein from the style canal of Gladiolus has been isolated by a one-step procedure involving lectin affinity chromatography, using the galactose-binding lectin from the small giant clam, Tridacna maxima, coupled to Sepharose 4B. The lectin binding is calcium-ion dependent, so that the arabinogalactan protein which is bound to the column in the presence of calcium can be eluted by washing the column with a calcium-free buffer. This method has a general utility for the purification of polysaccharides and glycoproteins containing β-linked galactosyl residues. © 1979.

引用

页码：41 / 45

页数：5

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