| アイテムタイプ |
紀要論文 / Departmental Bulletin Paper(1) |
| 公開日 |
2009-07-14 |
| タイトル |
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|
タイトル |
ユリ根中トリプシンインヒビター(LTI-II-4)の精製とその性質 |
| タイトル |
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|
タイトル |
Purification and characterization of a trypsin inhibitor (LTI-II-4) from Lily Bulb (Lilium lancifolium) |
|
言語 |
en |
| 言語 |
|
|
言語 |
jpn |
| 資源タイプ |
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|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
departmental bulletin paper |
| ID登録 |
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|
ID登録 |
10.14993/00000391 |
|
ID登録タイプ |
JaLC |
| 著者 |
寺田, 慎子
堀口, 美和
浅尾, 俊夫
高橋, 享子
Terada, Chikako
Asao, Toshio
|
| 抄録 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
Several proteins from lily bulb for foodstuffs showed strong inhibitory activity toward bovine trypsin. A trypsin inhibitor (LTI-II-4) was purified from lily bulb by a method including column chromatographies on CM-Sepharose CL-6B and DEAE-Sepharose GL-6B and high-pressure liquid chromatography. Purified LTI-II-4 had a molecular weight of 21,000. The amino acid composition was characterized by high contents of glycine, aspartic acid and serine. The inhibitor contained 4 halfcystines in its constituent amino acids. The N-terminal 25 and the C-terminal 3 residues of LTI-II-4 were sequenced. The Inhibitor was stable in a wide pH range under 50℃ and was unstable at the higher temperatures than 80℃. The reactivesite amino acid of LTI-II-4 was assumed to be lysine. The inhibitor didn't inhibit elastase and subtilisin. From these results, the inhibitor LTI-II-4 is assumed to belong to the Kunitz soybean trypsin inhibitor family. |
| 書誌情報 |
武庫川女子大学紀要. 自然科学編
巻 48,
p. 87-94,
発行日 2001-03-31
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| 出版者 |
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出版者 |
武庫川女子大学 |
| ISSN |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
0916-3123 |
| 書誌レコードID |
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|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AN10187277 |
P087-094.pdf (564.2 kB)
