Isolation and properties of a metalloproteinase from buckwheat (<i>Fagopyrum esculentum</i>) seeds
Mikhail A. Belozersky, Yakov E. Dunaevsky, Natalia Voskoboynikova
Biochemical Journal
Abstract
A homogeneous preparation of metalloproteinase, purified 1000-fold, was obtained from buckwheat (Fagopyrum esculentum) seeds. The Mr of the enzyme, determined by SDS/PAGE, was 34,000 (it was 39,000 by gel chromatography). Its pH optimum was 8.0-8.2 with 13 S globulin, from buckwheat seeds, as substrate. Atomic-absorption spectroscopy revealed the presence of one Zn2+ ion per enzyme molecule. The enzyme was completely inhibited by EDTA (1 mM), zincone (1 mM) and 1, 10-phenanthroline (1 mM). The metalloproteinase performed limited proteolysis of the following seed storage proteins: 13 S globulin from buckwheat seeds and 11 S globulin from soybean (Glycine max) seeds. It hydrolysed three peptide bonds formed by the amino groups of Leu15, Tyr16 and Phe25 in the oxidized B-chain of insulin. In its main properties the enzyme is similar to metalloproteinases of animal and bacterial origin.
Extracted Claims
4 claims extracted from this paper into the knowledge graph
metalloproteinase from buckwheat seeds hydrolyzes peptide bonds in 13 S globulin from buckwheat seeds and 11 S globulin from soybean seeds
“The metalloproteinase performed limited proteolysis of the following seed storage proteins: 13 S globulin from buckwheat seeds and 11 S globulin from soybean (Glycine max) seeds.”
metalloproteinase from buckwheat seeds hydrolyzes peptide bonds in the oxidized B-chain of insulin
“It hydrolysed three peptide bonds formed by the amino groups of Leu15, Tyr16 and Phe25 in the oxidized B-chain of insulin.”
metalloproteinase from buckwheat seeds hydrolyzes peptide bonds formed by the amino groups of Leu15, Tyr16, and Phe25 in the oxidized B-chain of insulin
“It hydrolysed three peptide bonds formed by the amino groups of Leu15, Tyr16 and Phe25 in the oxidized B-chain of insulin.”