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デルタビリルビンにおけるビリルビン・アルブミン共有結合部位の検討
https://kindai.repo.nii.ac.jp/records/2002263
https://kindai.repo.nii.ac.jp/records/2002263af095e04-34c4-4477-8bc2-81b576394d21
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
AN00063584-19930325-0073.pdf (513.6 KB)
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| Item type | ☆紀要論文 / Departmental Bulletin Paper(1) | |||||||||
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| 公開日 | 2025-01-17 | |||||||||
| タイトル | ||||||||||
| タイトル | デルタビリルビンにおけるビリルビン・アルブミン共有結合部位の検討 | |||||||||
| 言語 | ja | |||||||||
| タイトル | ||||||||||
| タイトル | Covalent binding site of bilirubin to albumin molecule in serum delta bilirubin | |||||||||
| 言語 | en | |||||||||
| 著者 |
村田, 尚美
× 村田, 尚美
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| 言語 | ||||||||||
| 言語 | jpn | |||||||||
| キーワード | ||||||||||
| 主題 | delta bilirubin, lysine, amino acid residue covalent bonding | |||||||||
| 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 | |||||||||
| 出版タイプ | ||||||||||
| 出版タイプ | AM | |||||||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||||||
| 出版者 名前 | ||||||||||
| 出版者 | 近畿大学医学会 | |||||||||
| 言語 | ja | |||||||||
| bibliographic_information |
ja : 近畿大学医学雑誌 en : Medical Journal of Kinki University 巻 18, 号 1, p. 73-82, 発行日 1993-03-25 |
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| ISSN | ||||||||||
| 収録物識別子タイプ | PISSN | |||||||||
| 収録物識別子 | 03858367 | |||||||||
| 内容記述 | ||||||||||
| 内容記述タイプ | Abstract | |||||||||
| 内容記述 | Delta bilirubin (Bδ) is a covalently albumin-bound bilirubin. A bilirubin binding amino acid residue of human albumin was identified using a large amount of Bδ fraction prepared from pooled icteric human serum. Bilirubin in pooled icteric human serum was first changed to an azoderivative by the addition of a diazo reagent to protect it from degradation. The azoderivative of Bδ (azoBδ) was prepared by affinity chromatography and high performance liquid chromatography (HPLC) using a preparative Micronex RP30 column. The BrCN-treated azo Bδ was digested with Achromobacter protease I and with Staphylococcal serine proteinase, sequentially. The fragmented peptides were fractionated by reversed phase HPLC using a μBondasphere column. A fraction which showed absorbance peaks both at 530 nm and at 215 nm was obtained and analyzed by a protein/peptide sequencer and an analyzer. The finally obtained peptide fraction was composed of amino acid residues 18 to 38 of human serum albumin. The detected molar amount of lysine 20 was about one third of that of the other amino acids which suggested the covalent bonding of bilirubin to lysine 20 of human serum albumin. | |||||||||
| 言語 | en | |||||||||
| 内容記述 | ||||||||||
| 内容記述タイプ | Other | |||||||||
| 内容記述 | 本文データはCiNiiから複製したものである。 | |||||||||
| 言語 | ja | |||||||||
