Purification and some properties of trypsin inhibitors from buckwheat seeds.

• KIYOHARA Toshifumi

  Laboratory of Biochemistry, Faculty of Agriculture, Kobe University

• IWASAKI Teruo

  Laboratory of Biochemistry, Faculty of Agriculture, Kobe University

抄録

Seven proteins which inhibited trypsin were purified from buckwheat seeds by (NH₄)₂SO₄ fractionation, gel-filtration, and DEAE- and CM-cellulose column chromatographies. The homogeneities of the purified inhibitors were established by polyacrylamide gel electrophoresis. These inhibitors were thermostable at acidic and neutral pH's and acted on trypsin more powerfully than on chymotrypsin. Three of them, BTI He, IIIb1, and IIIb2, were typical temporary inhibitors of trypsin and the others, BTI I, IIa, IIb, and Ilia, were permanent ones. These seven inhibitors had essentially no inhibitory activity against subtilisin, Aspergillus sydowi proteinase, neutral subtilopeptidase, papain, or pepsin.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 49 (3), 581-588, 1985

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390282681443100672
• NII論文ID: 130000026404
• DOI: 10.1271/bbb1961.49.581
• COI: 1:CAS:528:DyaL2MXitVSit70%3D
• ISSN: 18811280
• ISSN: 00021369
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可