PREPARATIVE PURIFICATION OF DIPEPTIDYL PEPTIDASE-IV

被引：6
|
作者：
SEIDL, R
SCHAEFER, W
机构：
[1] Max-Planck-Institute for Biochemistry, D-8033, Martinsried
来源：
PREPARATIVE BIOCHEMISTRY | 1991年 / 21卷 / 2-3期
关键词：
D O I：
10.1080/10826069108018009
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：
Dipeptidyl-Peptidase IV was purified from pig kidney by ammonium sulfate fractionation, gel filtration, QAE-cellulose chromatography and affinity columns with Gly-Pro- and Concanavalin A-Sepharose. The specific activity of the purified enzyme is 41.8 units/mg. Polyacrylamide gel electrophoresis and silver staining show a single band. The enzyme preparation is free of aminopeptidase and dipeptidase activity, proved fluorimetrically and by gas chromatography/mass spectrometry. The most important procedure for removal of contaminating enzyme activities is a stepwise NaCl-gradient on a QAE-ZetaPrep ion exchange disk.
引用
收藏
页码：141 / 150
页数：10
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