Activation of recombinant proenteropeptidase by duodenase

被引：34

作者：

Zamolodchikova, TS

Sokolova, EA

Lu, DS

Sadler, JE

机构：

[1] RAS, Shemyakin & Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia

[2] Eli Lilly & Co, Cardiovasc Res Div, Indianapolis, IN 46285 USA

[3] Washington Univ, Sch Med, Howard Hughes Med Inst, St Louis, MO 63110 USA

来源：

FEBS LETTERS | 2000年 / 466卷 / 2-3期

基金：

俄罗斯基础研究基金会;

关键词：

duodenase; proenteropeptidase activation; serine protease; duodenal mucosa;

D O I：

10.1016/S0014-5793(00)01092-9

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：

Duodenase, a serine proteinase from bovine Brunner's (duodenal) glands that was predicted to be a natural activator of enteropeptidase zymogen, cleaves and activates recombinant single-chain bovine proenteropeptidase (k(cat)/K-m = 2700 M-1 s(-1)). The measured rate of proenteropeptidase cleavage by duodenase was about 70-fold lower compared with the rate of trypsin-mediated cleavage of the zymogen, The role of duodenase is supposed to be the primary activator of proenteropeptidase maintaining a certain level of active enteropeptidase in the duodenum, A new scheme of proteolytic activation cascade of digestive proteases is discussed. (C) 2000 Federation of European Biochemical Societies.

引用

页码：295 / 299

页数：5

共 32 条

[21] ACTIVATION OF PANCREATIC ZYMOGENS - NORMAL ACTIVATION, PREMATURE INTRAPANCREATIC ACTIVATION, PROTECTIVE MECHANISMS AGAINST INAPPROPRIATE ACTIVATION [J].