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

页码：344 / 349

页数：6

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