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ID 30869
JaLCDOI
フルテキストURL
著者
Ikeda, Shogo Okayama University
Tsutsui, Ken 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
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
Web of Sience KeyUT