METALLOPROTEINASE FROM THE SEEDLINGS OF KALE (BRASSICA-OLERACEA L VAR SABELLICA) - PREPARATION, PARTIAL CHARACTERIZATION AND SUBSTRATE-SPECIFICITY

被引：5
|
作者：
WILIMOWSKAPELC, A [1 ]
DRYJANSKI, M [1 ]
ZAL, T [1 ]
WILUSZ, T [1 ]
机构：
[1] POLISH ACAD SCI,INST IMMUNOL & EXPTL THERAPY,PL-53114 WROCLAW,POLAND
来源：
PLANTA | 1991年 / 185卷 / 03期
关键词：
BRASSICA; METALLOPROTEINASE; PROTEOLYTIC SPECIFICITY (ENZYME);
D O I：
10.1007/BF00201054
中图分类号：
Q94 [植物学];
学科分类号：
071001 ;
摘要：
Metallo-proteinase from 8-d-old seedlings of kale was isolated. The enzyme was extracted with 1% NaCl, concentrated by ammonium sulfate and finally purified by high-performance liquid chromatography. The isolated enzyme had a molecular weight of 22.4 kDa and showed a maximum activity of pH 9.0 using casein as a substrate. Proteolytic activity of proteinase was inhibited by chelators. The inhibition by ethylenediaminetetraacetate (EDTA) was abolished by some divalent metals ions, especially by Zn2+. The enzyme showed activity against the synthetic peptides Suc-Ala-Ala-Pro-Leu-pNA and Suc-Ala-Ala-Pro-Phe-pNA, and hydrolized the following peptide bonds in the oxidized insulin B-chain: Leu6-Cya7, Leu15-Tyr16, Leu17-Val18 and Phe25-Tyr26.
引用
收藏
页码：344 / 349
页数：6
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