ID | 30869 |
JaLCDOI | |
フルテキストURL | |
著者 |
Ikeda, Shogo
Okayama University
Hatsushika, Masao
Okayama University
Watanabe, Sekiko
Okayama University
Oda, Takuzo
Okayama University
|
抄録 | 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. |
キーワード | retrovirus
gag protein
protein purification
high performance liquid chromatography
|
Amo Type | Article
|
出版物タイトル |
Acta Medica Okayama
|
発行日 | 1989-04
|
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 |
英語
|
論文のバージョン | publisher
|
査読 |
有り
|
PubMed ID | |
Web of Science KeyUT |