PURIFICATION OF WHEAT PROTEASES BY AFFINITY CHROMATOGRAPHY ON HEMOGLOBIN-SEPHAROSE COLUMN

被引：70

作者：

CHUA, GK

BUSHUK, W

机构：

[1] Protein Chemistry Laboratory, Department of Plant Science, University of Manitoba, Winnipeg 19, Man.

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 37卷 / 03期

基金：

加拿大自然科学与工程研究理事会;

关键词：

D O I：

10.1016/0006-291X(69)90950-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A rapid chromatographic procedure for the isolation and purification of proteases from malted wheat flour is described. The separation was achieved by passing the crude extract through a hemoglobin-Sepharose column. Unadsorbed proteins were eluted with the starting buffer. The adsorbed proteases were then eluted with O.1N acetic acid. Recoveries of proteins and proteolytic activity were over 90%. A two-fold increase in specific activity was achieved by this purification technique. Disc electrophoretic analyses showed that all of the non-proteolytic components were separated from the proteolytically active proteins. The active peak comprised three major and one minor proteins of similar mobility. © 1969.

引用

页码：545 / &

共 6 条

[1]

CHUA GK, 1969, 54 AACC M CHIC

[2] SELECTIVE ENZYME PURIFICATION BY AFFINITY CHROMATOGRAPHY [J].