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
43巻
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
43巻
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
38巻
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