SIMPLIFIED METHOD FOR THE PURIFICATION OF RIBOFLAVIN-BINDING PROTEIN FROM HENS EGG-YOLK

被引：23

作者：

MURTHY, US ^{[1
]}

SREEKRISHNA, K ^{[1
]}

ADIGA, PR ^{[1
]}

机构：

[1] INDIAN INST SCI,DEPT BIOCHEM,BANGALORE 560012,INDIA

来源：

ANALYTICAL BIOCHEMISTRY | 1979年 / 92卷 / 02期

关键词：

D O I：

10.1016/0003-2697(79)90668-7

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A simple and efficient procedure for the purification of the riboflavin-binding protein from hen's egg yolk is described. This method involves the removal by exclusion of lipoproteins and subsequent fractionation of soluble yolk proteins held on a DEAE-cellulose column by a salt gradient which is followed by purification by gel filtration on Sephadex G-100. The protein thus isolated is homogeneous by various physicoehemical, immunological, and functional criteria. © 1979.

引用

页码：345 / 350

页数：6

共 26 条

[1]

ANDREWS P, 1964, BIOCHEM J, V91, P22

[2] SYNTHESIS OF IMMOBILIZED FLAVIN DERIVATIVES AND THEIR USE IN PURIFICATION OF CHICKEN EGG-WHITE OVOFLAVOPROTEIN [J].