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

页码：141 / 150

页数：10