Purification and Some Properties of Trypsin Inhibitors from Buckwheat Seeds
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概要
- 論文の詳細を見る
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 pHs 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.
- 社団法人 日本農芸化学会の論文
著者
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KIYOHARA Toshifumi
Laboratory of Biochemistry, Faculty of Agriculture, Kobe University
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Iwasaki Teruo
Laboratory Of Biochemistly Faculty Of Agriculture Kobe University
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