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Purification of Protease from Vibrio cholerae O1 and its Partial Characterization
http://hdl.handle.net/10069/4605
http://hdl.handle.net/10069/4605cfd49990-c331-46f0-bf9b-02f5dd353004
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
tm34_03_06_t.pdf (720.4 kB)
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
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| 公開日 | 2006-04-26 | |||||
| タイトル | ||||||
| タイトル | Purification of Protease from Vibrio cholerae O1 and its Partial Characterization | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | departmental bulletin paper | |||||
| 著者 |
Ichinose, Yoshio
× Ichinose, Yoshio× Ehara, Masahiko× Utsunomiya, Akiyoshi |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | A protease produced by a clinical isolate of Vibrio cholerae O1 was purified to apparent homogeneity by ammonium sulfate fractionation, ultracentrifuge and succesive column chromatography on a Bio-gel A5m and a TSK gel G-3000SW HPLC column. The molecular weight of the purified protease was estimated to be 32,000 on the basis of its mobility on SDS-PAGE and was identical to HA/protease biochemically and physicochemically as previously reported (Booth et al., 1983; Honda et al., 1987). The hemagglutinin activity of purified protease, however, was not detected as previously described. The purified protease seemed to be identical biochemically and physicochemically but did not show the character of a bifunctional protein molecule. | |||||
| 書誌情報 |
熱帯医学 Tropical medicine 巻 34, 号 3, p. 121-125, 発行日 1992-09-30 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 03855643 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN00199644 | |||||
| 出版者 | ||||||
| 出版者 | 長崎大学熱帯医学研究所 | |||||
| 出版者別言語 | ||||||
| 値 | Institute of Tropical Medicine, Nagasaki University | |||||
| sortkey | ||||||
| 値 | P00121-P00125 | |||||
| 引用 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 熱帯医学 Tropical medicine 34(3). p121-125, 1992 | |||||
