書誌事項
- タイトル別名
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- Purification and Characterization of a
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抄録
A trypsin inhibitor was isolated and purified from the bran of rice, Oryza sativa, by extraction with 1% sodium chloride, heat treatment, ammonium sulfate precipitation, ion-exchange chromatog-raphy on a CM-Sephadex C-25 and gel filtration on a Sephadex G-75. The final preparation was homogeneous by electrophoretic analysis. Rice bran trypsin inhibitor (RBTI) had a molecular weight of about 14, 500 and an isoelectric point of 8.07. The amino acid composition was characterized by high contents of basic amino acids, aspartic acid, glutamic acid, proline and cystine. BRTI inhibited bovine trypsin at an inhibitor-enzyme molar ratio of 1:1.6. It displayed, however, nobility to inhibit α-chymotrypsin, pepsin, papain and subtilisin BPN'.
収録刊行物
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- Journal of Nutritional Science and Vitaminology
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Journal of Nutritional Science and Vitaminology 25 (3), 255-264, 1979
一般財団法人 学会誌刊行センター
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詳細情報 詳細情報について
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- CRID
- 1390001206324929152
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- NII論文ID
- 130001372045
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- NII書誌ID
- AA00703822
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- COI
- 1:CAS:528:DyaE1MXlslSlsb0%3D
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- ISSN
- 18817742
- 03014800
- http://id.crossref.org/issn/03014800
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- NDL書誌ID
- 2087858
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可