| JaLCDOI | 10.18926/AMO/30889 |
|---|---|
| フルテキストURL | fulltext.pdf |
| 著者 | Sumii, Hiroshi| Tsutsui, Ken| Hatsushika, Masao| Inoue, Hajime| Tanabe, Gozo| oda, Takuzo| |
| 抄録 | <p>Preparations of IgG2b purified from several mouse hybridoma clones were highly susceptible, compared to other subclasses, to peptic digestion under conditions usually used to prepare F (ab')2 fragments. Analyses of the digestion products revealed that no F (ab')2 was produced and that the main product was a Fab-like fragment. Demonstration of the hinge disulfides in the Fc portion clearly indicated that in IgG2b the primary peptic cleavage occurs on the NH2-terminal side of the inter-heavy chain disulfide bridge. The resulting Fab failed to bind with antigen, suggesting the importance of the CH1-hinge region in maintaining the native conformation of the antigen-binding site.</p> |
| キーワード | monoclonal antibody immunoglobulin G2b f (ab')2 peptic digestion maleimide compound |
| Amo Type | Article |
| 発行日 | 1989-06 |
| 出版物タイトル | Acta Medica Okayama |
| 巻 | 43巻 |
| 号 | 3号 |
| 出版者 | Okayama University Medical School |
| 開始ページ | 135 |
| 終了ページ | 141 |
| ISSN | 0386-300X |
| NCID | AA00508441 |
| 資料タイプ | 学術雑誌論文 |
| 言語 | English |
| 論文のバージョン | publisher |
| 査読 | 有り |
| PubMed ID | 2504035 |
| Web of Sience KeyUT | A1989AG01600001 |
| JaLCDOI | 10.18926/AMO/30869 |
|---|---|
| フルテキストURL | fulltext.pdf |
| 著者 | Ikeda, Shogo| Tsutsui, Ken| Hatsushika, Masao| Watanabe, Sekiko| Oda, Takuzo| |
| 抄録 | <p>The major gag protein (p34) of squirrel monkey retrovirus-H was purified in one chromatographic step by anion-exchange high performance liquid chromatography. The virus in a crude fraction was disrupted with Brij 35 in the presence of three kinds of protease inhibitors. The soluble virus lysate was injected into a Polyanion SI column, and p34 was eluted with a linear salt gradient. The recovery of the protein was about 60%. The purified p34 was nearly homogenous as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining.</p> |
| キーワード | retrovirus gag protein protein purification high performance liquid chromatography |
| Amo Type | Article |
| 発行日 | 1989-04 |
| 出版物タイトル | Acta Medica Okayama |
| 巻 | 43巻 |
| 号 | 2号 |
| 出版者 | Okayama University Medical School |
| 開始ページ | 127 |
| 終了ページ | 129 |
| ISSN | 0386-300X |
| NCID | AA00508441 |
| 資料タイプ | 学術雑誌論文 |
| 言語 | English |
| 論文のバージョン | publisher |
| 査読 | 有り |
| PubMed ID | 2786318 |
| Web of Sience KeyUT | A1989U578500007 |
| JaLCDOI | 10.18926/AMO/30311 |
|---|---|
| フルテキストURL | fulltext.pdf |
| 著者 | Ikeda, Shogo| Hatsushika, Masao| Shigehara, Tsuguya| Watanabe, Sekiko| Omura, Sachiko| Tsutsui, Ken| Oda, Takuzo| |
| 抄録 | <p>Simian virus 40 (SV40) large T antigen was partially purified from small amounts of SV40-infected and SV40-transformed cells by immunoaffinity chromatography with high recovery. T antigen, in both crude and partially purified states, was detected rapidly by a sensitive and quantitative enzyme-linked immunosorbent assay (ELISA). Stability of the partially purified T antigen was found to increase by addition of 0.01% bovine serum albumin (BSA).</p> |
| キーワード | SV40 T antigen affinity chromatography ELISA |
| Amo Type | Article |
| 発行日 | 1984-08 |
| 出版物タイトル | Acta Medica Okayama |
| 巻 | 38巻 |
| 号 | 4号 |
| 出版者 | Okayama University Medical School |
| 開始ページ | 341 |
| 終了ページ | 347 |
| ISSN | 0386-300X |
| NCID | AA00508441 |
| 資料タイプ | 学術雑誌論文 |
| 言語 | English |
| 論文のバージョン | publisher |
| 査読 | 有り |
| PubMed ID | 6093443 |
| Web of Sience KeyUT | A1984TG25900003 |