Purification of bovine alpha-lactalbumin by immobilized metal ion affinity chromatography

被引：14

作者：

Blomkalns, AL ^{[1
]}

Gomez, MR ^{[1
]}

机构：

[1] BAYLOR COLL MED,CHILDRENS NUTR RES CTR,HOUSTON,TX 77030

来源：

PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY | 1997年 / 27卷 / 04期

关键词：

D O I：

10.1080/10826069708001280

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The milk protein alpha-lactalbumin was isolated from bovine whey protein concentrate solution by immobilized metal ion affinity chromatography (IMAC) using Cu(II)-Chelating Sepharose Fast Flow. Stepwise pH (5.5-3.8) changes in sodium acetate buffer were used to elute the protein selectively, at which time it was concentrated and reapplied to an uncharged Chelating Sepharose Fast Flow column to remove the contaminating Cu(II) ions. A purity of 90% and recovery of 80% was achieved. The described method appears to be suitable for isolation of alpha-lactalbumin in a form adequate for milk formula engineering.

引用

页码：219 / 226

页数：8

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