HIGH-YIELD PURIFICATION OF GLUCOKINASE FROM RAT-LIVER

被引：11
|
作者：
MIWA, I
MITSUYAMA, S
TOYODA, Y
MURATA, T
OKUDA, J
机构：
[1] Department of Clinical Biochemistry, Faculty of Pharmacy, Meijo University., Nagoya
来源：
PREPARATIVE BIOCHEMISTRY | 1990年 / 20卷 / 02期
关键词：
D O I：
10.1080/00327489008050187
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 and reliable method for the purification of rat liver glucokinase was developed. The procedure consists of DEAE-cellulose ion-exchange chromatography, Phenyl-Sepharose hydrophobic interaction chromatography, DEAE-Affi Gel Blue dye-ligand chromatography, and duplicate steps of glucosamine-Sepharose affinity chromatography. Glucokinase was purified to a specific activity of 290 units/mg protein in a yield of 55% in 6 days. The final enzyme preparations were completely homogeneous in most experiments as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The estimated molecular weight (51,000) and sigmoidal saturation function for glucose of purified glucokinase were in good agreement with published data. © 1990, Taylor & Francis Group, LLC. All rights reserved.
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页码：163 / 178
页数：16
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