ELECTROCHEMICAL INVESTIGATION OF ENZYME CATALYZED-HYDROLYSIS AND SYNTHESIS OF PEPTIDES USING PEPTIDYL-4-NITROANILIDES AS SUBSTRATES

被引：5

作者：

HEIDUSCHKA, P

DITTRICH, J

机构：

[1] Pädagogische Hochschule Halle-Köthen, Sektion Chemie, Halle/S, DDR-4002

来源：

BIOELECTROCHEMISTRY AND BIOENERGETICS | 1990年 / 24卷 / 02期

关键词：

D O I：

10.1016/0302-4598(90)85024-C

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：

The hydrolysis and synthesis of peptide catalysed by the serine protease dipeptidylpeptidase IV (E.C. 3.4.14.5) have been examined by differential pulse polarography (DPP) at the dropping mercury electrode. Gly-Pro-4-nitroanilide was used as the substrate. Both the latter and its hydrolysis product 4-nitroaniline are well detectable by DPP. The kinetic parameters of the hydrolysis have been determined in pure phosphate buffer and its mixtures with glycerol or DMSO. Further applications of DPP for measurements in coloured solutions and detection of the formation of the peptide bond are described. © 1990.

引用

页码：231 / 239

页数：9