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| ファイル | 記述 | サイズ | フォーマット | |
|---|---|---|---|---|
| j.bbrc.2012.07.138.pdf | 231.9 kB | Adobe PDF | 見る/開く |
| タイトル: | A P39R mutation at the N-terminal domain of human αB-crystallin regulates its oligomeric state and chaperone-like activity. |
| 著者: | Numoto, Nobutaka Kita, Akiko    https://orcid.org/0000-0002-5174-6238 (unconfirmed)Fujii, Noriko Miki, Kunio |
| 著者名の別形: | 喜田, 昭子 |
| キーワード: | Small heat shock protein Molecular chaperone Quaternary assembly Protein aggregation Secondary structure Cataract |
| 発行日: | 31-Aug-2012 |
| 出版者: | Elsevier Inc. |
| 誌名: | Biochemical and biophysical research communications |
| 巻: | 425 |
| 号: | 3 |
| 開始ページ: | 601 |
| 終了ページ: | 606 |
| 抄録: | Recent structure analyses of αB-crystallin have proposed some models of the N-terminal domain and the manner of oligomerization, whereas the effects of the significantly high content of Pro residues at the N-terminal domain remain unclear. We report the properties of a novel P39R mutant of αB-crystallin. The content of α-helix was increased, and the molecular size of the P39R mutant was larger than that of wild-type αB-crystallin. A slight loss of chaperone-like activity was observed using alcohol dehydrogenase (ADH), while a significant increase was detected by insulin assay. The Pro residue at the N-terminal domain of αB-crystallin is important for oligomerization and function. |
| 著作権等: | © 2012 Elsevier Inc. This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
| URI: | http://hdl.handle.net/2433/167502 |
| DOI(出版社版): | 10.1016/j.bbrc.2012.07.138 |
| PubMed ID: | 22877753 |
| 出現コレクション: | 学術雑誌掲載論文等 |
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