書誌事項
- タイトル別名
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- Purification and Characterization of a Cysteine Proteinase Inhibitor(Cystatin) from Seeds of Foxtail Millet, Setaria italica.
- アワ シュシ カラ ノ システインプロテイナーゼインヒビタ ノ セイセイ ト セイシツ
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A cysteine proteinase inhibitor was purified from the extract of seeds of foxtail millet, Setaria italica, to an electrophoretically homogeneous protein by heat treatment, salting-out, ion-exchange chromatography on DEAE-Sepharose CL-6 B, gel filtration on Sephadex G-50, and chromatofocusing on PBE 94. The inhibitor (FMCPI) was a single polypeptide with a molecular weight of 12000 and an isoelectric point of 5.2. It possessed the amino acid composition characterized by fairly high contents of aspartic acid, glutamic acid, and alanine and by no half-cystine. FMCPI was relatively thermostable since it maintained more than 50% of the original activity after treatment of 100°C for 20min at pH 2 or 7. However, the inhibitor almost lost its whole activity by the above treatment at pH 10. FMCPI inhibited papain in a 1:1 protein molar ratio: the Ki value was 2.4×10-11M. Complex formation between FMCPI and papain derivatives demonstrated that the inhibitor was capable of combining with even a papain molecule without the catalytic ability.
収録刊行物
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- 日本食品科学工学会誌
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日本食品科学工学会誌 47 (2), 105-111, 2000
公益社団法人 日本食品科学工学会
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詳細情報 詳細情報について
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- CRID
- 1390282681387008000
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- NII論文ID
- 10007505303
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- NII書誌ID
- AN10467499
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- ISSN
- 18816681
- 1341027X
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- NDL書誌ID
- 5277515
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
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