title: Metallo-proteinase from the seedlings of kale (Brassica oleracea L. var. sabellica): : Preparation, partial characterization and substrate specificity.
abstract: 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 at 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 Zn(2+). 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.
authors.affiliation: Institute of Biochemistry, University of Wrocław, Tamka 2, PL-53114, Wrocław, Poland.
authors.forename: A
authors.initials: A
authors.lastname: Wilimowska-Pelc
authors.forename: M
authors.initials: M
authors.lastname: Dryjański
authors.forename: T
authors.initials: T
authors.lastname: Zal
authors.forename: T
authors.initials: T
authors.lastname: Wilusz