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卵白 Flavoprotein の化学修飾(生活科学)
https://kpu.repo.nii.ac.jp/records/5262
https://kpu.repo.nii.ac.jp/records/52623d600e0c-0dba-4a67-b376-64eaaf12af9a
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
KJ00000079388.pdf (325.2 kB)
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| Item type | [ELS]紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-02-20 | |||||
| タイトル | ||||||
| タイトル | 卵白 Flavoprotein の化学修飾(生活科学) | |||||
| 言語 | ja | |||||
| その他（別言語等） | ||||||
| その他のタイトル | Chemical Modification of Egg White Flavoprotein (LIVING SCIENCE) | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | jpn | |||||
| 資源タイプ | ||||||
| 資源タイプ | departmental bulletin paper | |||||
| 著者 |
河端, 信
× 河端, 信× 田口, 邦子 |
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| 抄録(英) | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | Flavin-binding capacity of chicken egg white apoprotein and its chemically modified derivatives were investigated. No major change was observed in the flavin-binding capacity of acetylated, succinylated and carbamylated apoprotein as compared with that of native apoprotein. The flavin-binding capacity of apoprotein was destroyed by reduction, S-carboxymethylation, iodination and modification of tryptophane residue with Koshland's reagent. 8 M-Urea treatment also inhibits the flavin-binding but this inhibition was reversed after dialysis. We conclude from the experiments described above that the flavin-binding site of apoprotein are tryptophane or histidine residue. The binding site requires tertiary structure which is supported by hydrogen bond and is stabilized by disulfide bond of the peptide chain. | |||||
| 言語 | en | |||||
| 書誌情報 |
ja : 京都府立大学学術報告. 理学・生活科学 en : The scientific reports of the Kyoto Prefectural University. Natural science and living science 巻 24, p. 7-10, 発行日 1973-10-31 |
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| 雑誌書誌ID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN00062300 | |||||
| ISSN | ||||||
| 収録物識別子タイプ | PISSN | |||||
| 収録物識別子 | 0075739X | |||||
