書誌事項
- タイトル別名
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- Protease Inhibitor in Passion Fruit.
- パッション フルーツチュウ ノ プロテアーゼ インヒビター
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説明
A protease inhibitor (PEPI) was isolated and purified from the juice of the passion fruit (Passiflora edulis Sim) by DEAE-Sephacel and trypsin-Sepharose 4B column chromatography. The molecular weight of PEPI was found to be 25 kDa by gel filtration. PEPI exhibited a single band in native and SDSPAGE gels under non-reducing conditions. Under reducing conditions in SDS-PAGE gel, PEPI exhibited three protein bands with estimated molecular weights of 25, 22, 18 kDa, respectively. The three protein bands were stained with PAS reagent. PEPI inhibited trypsin and chymotrypsin activities, but did not inhibit papain activity. The trypsin-inhibitory activity of PEPI was heat-stable, retaining 50% of the original activity even after exposure to 100°C for 10 min. The trypsin-inhibitory activity of PEPI was stable over a pH range of 2-12.
収録刊行物
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- 日本栄養・食糧学会誌
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日本栄養・食糧学会誌 46 (5), 409-415, 1993
公益社団法人 日本栄養・食糧学会
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詳細情報 詳細情報について
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- CRID
- 1390282681269622912
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- NII論文ID
- 130000853955
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- NII書誌ID
- AN00311992
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- ISSN
- 18832849
- 02873516
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- NDL書誌ID
- 3853135
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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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- 抄録ライセンスフラグ
- 使用不可