PROTEOLYTIC-ENZYMES IN GREEN WHEAT-LEAVES .3. INACTIVATION OF ACID PROTEINASE-II BY DIAZOACETYL-DL-NORLEUCINE METHYL-ESTER AND 1,2-EPOXY-3-(PARA-NITROPHENOXY)-PROPANE

被引：4

作者：

FRITH, GJT

PEOPLES, MB

DALLING, MJ

机构：

[1] Plant Sciences Section, School of Agriculture and Forestry, University of Melbourne

来源：

PLANT AND CELL PHYSIOLOGY | 1978年 / 19卷 / 05期

关键词：

1,2-Epoxy-3-(p-nitrophenoxy)-propane; Acid proteinase; Diazoacetyl-DL-norleucine methyl ester; Inhibition; Wheat leaves;

D O I：

10.1093/oxfordjournals.pcp.a075656

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Acid proteinase II isolated from green wheat leaves in a purified form was rapidly inactivated at pH=5.5 to 6.0 by a 50-fold molar excess of diazoacetyl-DL-norleucine methyl ester (DAN) in the presence of cupric ions which were essential for inactivation. The acid proteinase was also inactivated by reaction with 1,2-epoxy-3-(p-nitrophenoxy)-propane (EPNP). The inactivation by EPNP was much slower than by DAN and the half-life of the activity was 24 hr. © 1978 Oxford University Press.

引用

页码：819 / 824

页数：6

共 17 条

[1] AN ASPARTIC ACID RESIDUE AT ACTIVE SITE OF PEPSIN - ISOLATION AND SEQUENCE OF HEPTAPEPTIDE [J].