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Some properties of Dirofilariaimmitis acid proteinase as compared with those of mammalian cathepsin D and pepsin
http://hdl.handle.net/10087/2050
http://hdl.handle.net/10087/2050a61e12c5-2f49-4f16-9834-c60ce345d726
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
KJ00004436378.pdf (404.5 kB)
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2007-12-20 | |||||
| タイトル | ||||||
| タイトル | Some properties of Dirofilariaimmitis acid proteinase as compared with those of mammalian cathepsin D and pepsin | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | Dirofilaria immitis | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | acid proteinase | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | aspartic proteinase | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | cathepsin D | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | pepsin | |||||
| 著者 |
Sato, Kumiko
× Sato, Kumiko× Kara, Fumiko |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Some properties of Dirofilaria immitis acid proteinase were compared with mammalian cathepsin D and pepsin. The optimum pH of D. immitis acid proteinase was in the range of pH 2.8 to 3.4, whereas mammalian cathepsin D and porcine pepsin were 3.0 - 4.6 and around 2.0, respectively. When incubating in neutral pH at 50℃ for 10min, the activity of D. immitis proteinase was reduced to about 75% of the initial level, although that of cathepsin D did not change and that of pepsin was completely destroyed. D. immitis proteinase and cathepsin D hydrolyzed well human hemoglobin and myoglobin, whereas pepsin hydrolyzed human hemoglobin, bovine hemoglobin and cytochrome C. Pepstatin, a potent inhibitor of mammalian cathepsin D completely inhibited these three enzymes. However, the effect of pepstatin was abolished strongest on pepsin (5 × 10^<-8>). About 90% of the activity of pepsin was inactivated by diazoacetyl-DL-norleucine methyl ester (DAN) for 10min after beginning the reaction. Under the same condition, D. immitis proteinase was inactivated gradually, about 50% of the initial activity was inactivated 60min after the beginning of the experiment. However, cathepsin D was never affected by DAN even for after a 60min incubation. About 30% of the activity of pepsin was inactivated by first incubating the enzyme with 1.2-epoxy-3-(P-nitrophenoxy)-propane at 37℃ for 10 min, although D. immitis proteinase and cathepsin D were not affected. In conclusion, we confirmed that the D. immitis proteinase belongs to the aspartic proteinase group and is an intermediate type between cathepsin D and pepsin. | |||||
| 書誌情報 |
群馬大学医療技術短期大学部紀要 巻 15, p. 145-151, 発行日 1995-03-31 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0389-7540 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN00068340 | |||||
| フォーマット | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
| 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 | |||||
| 出版者 | ||||||
| 出版者 | 群馬大学医療技術短期大学部 | |||||
| 資源タイプ | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | Departmental Bulletin Paper | |||||
| 更新日 | ||||||
| 日付 | 2017-03-27 | |||||
| 日付タイプ | Created | |||||
