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Isolation and properties of anionic protease inhibitors from buckwheat seeds
Author(s) -
Dunaevsky Y. E.,
Pavlukova E. B.,
Belozersky M. A.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201692
Subject(s) - papain , chemistry , subtilisin , trypsin , protease , valine , isoleucine , chromatography , chymotrypsin , amino acid , biochemistry , molecular mass , enzyme , leucine
Three protease inhibitors (BWI‐1, BWI‐2 and BWI‐4) from buckwheat seeds were purified to homogeneity and characterized. Their molecular masses were 7.7‐9.2 kDa according to gel‐filtration and mass spectrometry. Amino acid analysis revealed a high content of glutamic acid and valine and a low content of isoleucine, aromatic and sulfur‐containing amino acids. Data illustrating the temperature and the pH stability of the inhibitors are presented. Each of the inhibitors formed a inhibitor complex with trypsin in a molar ratio 1:1 and contained an Arg residue at the reactive site. In addition to trypsin, BWI‐1 and BWI‐2 inhibited chymotrypsin, however, less effectively. None of the isolated inhibitors suppressed activity of papain, leukocyte elastase, pepsin and subtilisin.