WEKO3
アイテム
Affinity Chromatographic Purification and Characterization of Sialic Acid Binding Proteins in Bovine Kidney
http://hdl.handle.net/10083/808
http://hdl.handle.net/10083/808ccf50dd5-8cc2-4bc7-9051-59aa241884d5
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
KJ00004470757.pdf (933.6 kB)
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2007-04-23 | |||||
| タイトル | ||||||
| タイトル | Affinity Chromatographic Purification and Characterization of Sialic Acid Binding Proteins in Bovine Kidney | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源 | http://purl.org/coar/resource_type/c_6501 | |||||
| タイプ | departmental bulletin paper | |||||
| 著者 |
Kojima, Kyoko
× Kojima, Kyoko× Adachi, Masami× Ogawa, Haruko× Seno, Nobuko× Matsumoto, Isamu |
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| 著者(ヨミ) | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 70440 | |||||
| 姓名 | コジマ, キョウコ | |||||
| 著者(ヨミ) | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 70441 | |||||
| 姓名 | アダチ, マサミ | |||||
| 著者(ヨミ) | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 70442 | |||||
| 姓名 | オガワ, ハルコ | |||||
| 著者(ヨミ) | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 70443 | |||||
| 姓名 | セノ, ノブコ | |||||
| 著者(ヨミ) | ||||||
| 識別子Scheme | WEKO | |||||
| 識別子 | 70444 | |||||
| 姓名 | マツモト, イサム | |||||
| 内容記述 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | Sialic acid binding proteins were purified from bovine kidney by successive affinity chromatography on fetuin and heparin clumns. The proteins adsorbed calcium-dependently on fetuin-Sepharose were further subjected to affinity chromatography on heparin-Sepharose. The proteins were separated into two fractions, fraction I and fraction II, by elution with 2mM EDTA and 0.3M NaCl, respectively. The affinity purified fractions had the binding activities to biotinylated fetuin in a polystyrene microtiter well, but not hemagglutinating activities. Inhibition assay of the binding revealed that N-acetylneuraminic acid is the most potent inhibitor for both fractions among the monosaccharides tested. Upon SDS-polyacrylamide gel electrophoresis, fraction-I gave three bands corresponding to 37kDa, 43kDa and 50kDa proteins and fraction-II four bands corresponding to 38kDa, 39kDa, 41kDa and 74kDa proteins. The proteins were electroblotted onto a polyvinylidene difluoride membrane and then subjected to the direct chemical analyses and the binding studies using horseradish peroxidase (HRP)-labeled binding probes. All the proteins had\ similar amino acid compositions and were N-terminally blocked. Neither of all proteins was stained with HRP-concanavalin A and HRP-peanut agglutinin, suggesting that they are not glycosylated. All of them were stained with HRP-fetuin and HRP-anhydrotrypsin. The results suggest that they have the carbohydrate recognition domain specific to N-acetylneuraminic acid and are the fragments produced by proteolytic digestion with endogenous trypsin family proteases in the kidney. |
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| 書誌情報 |
お茶の水女子大學自然科學報告 巻 42, 号 1, p. 1-11, 発行日 1991-07-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 00298190 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN00033958 | |||||
| フォーマット | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
| 形態 | ||||||
| 933629 bytes | ||||||
| 日本十進分類法 | ||||||
| 主題Scheme | NDC | |||||
| 主題 | 400 | |||||
| 出版者 | ||||||
| 出版者 | お茶の水女子大学 | |||||
| 資源タイプ | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 紀要論文 | |||||
| 資源タイプ・ローカル | ||||||
| 紀要論文 | ||||||
| 資源タイプ・NII | ||||||
| Departmental Bulletin Paper | ||||||
| 資源タイプ・DCMI | ||||||
| text | ||||||
| 資源タイプ・ローカル表示コード | ||||||
| 03 | ||||||
| 所属 | ||||||
| From the Department of Chemistry, Faculty of Science, Ochanomizu University | ||||||
| 所属 | ||||||
| From the Department of Chemistry, Faculty of Science, Ochanomizu University | ||||||
| 所属 | ||||||
| From the Department of Chemistry, Faculty of Science, Ochanomizu University | ||||||
| 所属 | ||||||
| From the Department of Chemistry, Faculty of Science, Ochanomizu University | ||||||
| 所属 | ||||||
| From the Department of Chemistry, Faculty of Science, Ochanomizu University | ||||||
