WEKO3
アイテム
ラツト肝臓リソソームに存在するアリルアミダーゼの精製と性質(自然科学編)
https://nakamura-u.repo.nii.ac.jp/records/2015
https://nakamura-u.repo.nii.ac.jp/records/2015c2f5498a-bf10-4a09-a52e-eb9c23a53ad2
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
KJ00000735297.pdf (569.0 kB)
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| アイテムタイプ | [ELS]紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-03-14 | |||||
| タイトル | ||||||
| タイトル | ラツト肝臓リソソームに存在するアリルアミダーゼの精製と性質(自然科学編) | |||||
| タイトル | ||||||
| タイトル | Purification and Characterization of a Lysosomal Arylamidase from Rat Liver | |||||
| 言語 | en | |||||
| 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 | |||||
| 雑誌書誌ID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN0017924X | |||||
| 著者 |
広井, 祐三
× 広井, 祐三× 大和, 孝子× HIROI, Yuzo× YAMATO, Takako |
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| 著者所属(日) | ||||||
| 値 | 中村学園大学・短期大学食物栄養学科・食物栄養科 | |||||
| 著者所属(日) | ||||||
| 値 | 中村学園大学・短期大学食物栄養学科・食物栄養科 | |||||
| 著者所属(英) | ||||||
| 言語 | en | |||||
| 値 | Nakamura Gakuen College and Nakamura Gakuen Junior College | |||||
| 著者所属(英) | ||||||
| 言語 | en | |||||
| 値 | Nakamura Gakuen College and Nakamura Gakuen Junior College | |||||
| 抄録(英) | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | Rat liver lysosomes contain an arylamidase which has molecular weight of 135,000, and is separated into seven forms under isoelectric focusing. One form of these arylamidases, having isoelectric point of 7.8(form IV), was purified from rat liver by conventional chromatographic techniques. Final preparation of form VI appeared homogeneous by polyacrylamide disk electrophoresis and consisted of three identical polypeptide chain, as judged by disk electrophoresis in the presence of sodium dodecyl sulfate. The enzyme hydrolyzed naphthylamides of neutral amino acids but did not hydrolyze naphthylamides of basic, aromatic and acidic amino acids. The pH optimum for the hydrolysis of valine-β-naphthylamide was 7.0. The enzyme was inhibited by sulfhydryl-reactive reagents, TPCK, TLCK, and protease inhibitors of microbial origin, but not by puromycin. The enzyme hydrolyzed dipeptides and tripeptides. The pH optimum of the enzyme for the hydrolysis of Leu-Leu was 7.5. Physiological roles of the enzyme in lysosomes are discussed. | |||||
| 書誌情報 |
中村学園研究紀要 en : Bulletin of Nakamura Gakuen University and Nakamura Gakuen Junior College 巻 24, 発行日 1992-02-28 |
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| 表示順 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 25 | |||||
| アクセション番号 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | KJ00000735297 | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 02887312 | |||||
